ExplorEnz: EC 3.1.3*

3.1.3.1

Accepted name:

alkaline phosphatase

Reaction:

a phosphate monoester + H₂O = an alcohol + phosphate

Other name(s):

alkaline phosphomonoesterase; phosphomonoesterase; glycerophosphatase; alkaline phosphohydrolase; alkaline phenyl phosphatase; orthophosphoric-monoester phosphohydrolase (alkaline optimum)

Systematic name:

phosphate-monoester phosphohydrolase (alkaline optimum)

Comments:

Wide specificity. Also catalyses transphosphorylations. The human placental enzyme is a zinc protein. Some enzymes hydrolyse diphosphate (cf. EC 3.6.1.1 inorganic diphosphatase)

References:

1.	Engström, L. Studies on calf-intestinal alkaline phosphatase. I. Chromatographic purification, microheterogeneity and some other properties of the purified enzyme. Biochim. Biophys. Acta 52 (1961) 36–48. [PMID: 13890304]
2.	Harkness, D.R. Studies on human placental alkaline phosphatase. II. Kinetic properties and studies on the apoenzyme. Arch. Biochem. Biophys. 126 (1968) 513–523. [PMID: 4970479]
3.	Malamy, M.H. and Horecker, B.L. Purification and crystallization of the alkaline phosphatase of Escherichia coli. Biochemistry 3 (1964) 1893–1897. [PMID: 14269306]
4.	Morton, R.K. Alkaline phosphatase of milk. 2. Purification of the enzyme. Biochem. J. 55 (1953) 795–800. [PMID: 13115375]
5.	Stadtman, T.C. Alkaline phosphatases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 5, Academic Press, New York, 1961, pp. 55–71.

[EC 3.1.3.1 created 1961]

3.1.3.2

Accepted name:

acid phosphatase

Reaction:

a phosphate monoester + H₂O = an alcohol + phosphate

Other name(s):

acid phosphomonoesterase; phosphomonoesterase; glycerophosphatase; acid monophosphatase; acid phosphohydrolase; acid phosphomonoester hydrolase; uteroferrin; acid nucleoside diphosphate phosphatase; orthophosphoric-monoester phosphohydrolase (acid optimum)

Systematic name:

phosphate-monoester phosphohydrolase (acid optimum)

Comments:

Wide specificity. Also catalyses transphosphorylations.

References:

1.	Joyce, B.K. and Grisolia, S. Purification and properties of a nonspecific acid phosphatase from wheat germ. J. Biol. Chem. 235 (1960) 2278–2281. [PMID: 14408027]
2.	Kuo, M.-H. and Blumenthal, H.J. Purification and properties of an acid phosphomonoesterase from Neurospora crassa. Biochim. Biophys. Acta 52 (1961) 13–29. [PMID: 14460641]
3.	Tsuboi, K.K., Wiener, G. and Hudson, P.B. Acid phosphatase. VII. Yeast phosphomonoesterase; isolation procedure and stability characteristics. J. Biol. Chem. 224 (1957) 621–635. [PMID: 13405892]

[EC 3.1.3.2 created 1961]

3.1.3.3

Accepted name:

phosphoserine phosphatase

Reaction:

O-phospho-L(or D)-serine + H₂O = L(or D)-serine + phosphate

Systematic name:

O-phosphoserine phosphohydrolase

References:

1.	Borkenhagen, L.F. and Kennedy, E.P. The enzymatic exchange of L-serine with O-phospho-L-serine catalyzed by a specific phosphatase. J. Biol. Chem. 234 (1959) 849–853. [PMID: 13654276]
2.	Byrne, W.L. Glucose-6-phosphatase and phosphoserine phosphatase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 5, Academic Press, New York, 1961, pp. 73–78.
3.	Neuhaus, F.C. and Byrne, W.L. Metabolism of phosphoserine. II. Purification and properties of O-phosphoserine phosphatase. J. Biol. Chem. 234 (1959) 113–121. [PMID: 13610904]

[EC 3.1.3.3 created 1961]

3.1.3.4

Accepted name:

phosphatidate phosphatase

Reaction:

a 1,2-diacylglycerol 3-phosphate + H₂O = a 1,2-diacyl-sn-glycerol + phosphate

Glossary:

a 1,2-diacylglycerol 3-phosphate = a 3-sn-phosphatidate
a 1,2-diacyl-sn-glycerol = diacylglycerol = DAG

Other name(s):

phosphatic acid phosphatase; acid phosphatidyl phosphatase; phosphatic acid phosphohydrolase; PAP; Lipin

Systematic name:

diacylglycerol-3-phosphate phosphohydrolase

Comments:

This enzyme catalyses the Mg²⁺-dependent dephosphorylation of a 1,2-diacylglycerol-3-phosphate, yielding a 1,2-diacyl-sn-glycerol (DAG), the substrate for de novo lipid synthesis via the Kennedy pathway and for the synthesis of triacylglycerol. In lipid signalling, the enzyme generates a pool of DAG to be used for protein kinase C activation. The mammalian enzymes are known as lipins.

References:

1.	Smith, S.W., Weiss, S.B. and Kennedy, E.P. The enzymatic dephosphorylation of phosphatidic acids. J. Biol. Chem. 228 (1957) 915–922. [PMID: 13475370]
2.	Carman, G.M. and Han, G.S. Phosphatidic acid phosphatase, a key enzyme in the regulation of lipid synthesis. J. Biol. Chem. 284 (2009) 2593–2597. [PMID: 18812320]

[EC 3.1.3.4 created 1961, modified 2010]

3.1.3.5

Accepted name:

5′-nucleotidase

Reaction:

a 5′-ribonucleotide + H₂O = a ribonucleoside + phosphate

Other name(s):

uridine 5′-nucleotidase; 5′-adenylic phosphatase; adenosine 5′-phosphatase; AMP phosphatase; adenosine monophosphatase; 5′-mononucleotidase; AMPase; UMPase; snake venom 5′-nucleotidase; thimidine monophosphate nucleotidase; 5′-AMPase; 5′-AMP nucleotidase; AMP phosphohydrolase; IMP 5′-nucleotidase

Systematic name:

5′-ribonucleotide phosphohydrolase

Comments:

Wide specificity for 5′-nucleotides.

References:

1.	Gulland, J.M. and Jackson, E.M. 5-Nucleotidase. Biochem. J. 32 (1938) 597–601. [PMID: 16746659]
2.	Heppel, L.A. and Hilmoe, R.J. Purification and properties of 5-nucleotidase. J. Biol. Chem. 188 (1951) 665–676. [PMID: 14824154]
3.	Segal, H.L. and Brenner, B.M. 5′-Nucleotidase of rat liver microsomes. J. Biol. Chem. 235 (1960) 471–474. [PMID: 14444527]

[EC 3.1.3.5 created 1961]

3.1.3.6

Accepted name:

3′-nucleotidase

Reaction:

a 3′-ribonucleotide + H₂O = a ribonucleoside + phosphate

Other name(s):

3′-mononucleotidase; 3′-phosphatase; 3′-ribonucleotidase

Systematic name:

3′-ribonucleotide phosphohydrolase

Comments:

Wide specificity for 3′-nucleotides.

References:

1.	Shuster, L. and Kaplan, N.O. A specific b nucleotidase. J. Biol. Chem. 201 (1953) 535–546. [PMID: 13061389]

[EC 3.1.3.6 created 1961]

3.1.3.7

Accepted name:

3′(2′),5′-bisphosphate nucleotidase

Reaction:

adenosine 3′,5′-bisphosphate + H₂O = AMP + phosphate

Other name(s):

phosphoadenylate 3′-nucleotidase; 3′-phosphoadenylylsulfate 3′-phosphatase; 3′(2′),5′-bisphosphonucleoside 3′(2′)-phosphohydrolase

Systematic name:

adenosine-3′(2′),5′-bisphosphate 3′(2′)-phosphohydrolase

Comments:

Also acts on 3′-phosphoadenylyl sulfate, and on the corresponding 2′-phosphates.

References:

1.	Brungraber, E.G. Nucleotides involved in the enzymatic conjugation of phenols with sulfate. J. Biol. Chem. 233 (1958) 472–477. [PMID: 13563523]
2.	Farooqui, A.A. and Balasubramanian, A.S. Enzymatic dephosphorylation 3′-phosphoadenosine 5′-phosphosulfate to adenosine 5′-phosphosulfate in sheep brain. Biochim. Biophys. Acta 198 (1970) 56–65. [PMID: 4313079]
3.	Ramaswamy, S.G. and Jakoby, W.B. (2′)3′,5′-Bisphosphate nucleotidase. J. Biol. Chem. 262 (1987) 10044–10047. [PMID: 3038862]
4.	Tsang, M. L.-S. and Schiff, J.A. Properties of enzyme fraction A from Chlorella and copurification of 3′ (2′), 5′-biphosphonucleoside 3′ (2′)-phosphohydrolase, adenosine 5′phosphosulfate sulfohydrolase and adenosine-5′-phosphosulfate cyclase activities. Eur. J. Biochem. 65 (1976) 113–121. [PMID: 179817]

[EC 3.1.3.7 created 1961]

3.1.3.8

Accepted name:

3-phytase

Reaction:

myo-inositol hexakisphosphate + H₂O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate

Other name(s):

1-phytase; phytase; phytate 1-phosphatase; phytate 6-phosphatase

Systematic name:

myo-inositol-hexakisphosphate 3-phosphohydrolase

References:

1.	Cosgrove, D.J. Ion-exchange chromatography of inositol polyphosphates. Ann. N.Y. Acad. Sci. 165 (1969) 677–686. [PMID: 4310381]
2.	Johnson, L.F. and Tate, M.E. The structure of myo-inositol pentaphosphates. Ann. N.Y. Acad. Sci. 165 (1969) 526–532. [PMID: 4310376]
3.	Irving, G.C.J. and Cosgrove, D.J. Inositol phosphate phosphatases of microbiological origin: the inositol pentaphosphate products of Aspergillus ficuum phytases. J. Bacteriol. 112 (1972) 434–438. [PMID: 4342816]
4.	Cosgrove, D.J. Inositol Phosphates: Their Chemistry, Biochemistry, and Physiology, Elsevier, Amsterdam, 1980.

[EC 3.1.3.8 created 1961, modified 1976, modified 2002]

3.1.3.9

Accepted name:

glucose-6-phosphatase

Reaction:

D-glucose 6-phosphate + H₂O = D-glucose + phosphate

Other name(s):

glucose 6-phosphate phosphatase

Systematic name:

D-glucose-6-phosphate phosphohydrolase

Comments:

Wide distribution in animal tissues. Also catalyses potent transphosphorylations from carbamoyl phosphate, hexose phosphates, diphosphate, phosphoenolpyruvate and nucleoside di- and triphosphates, to D-glucose, D-mannose, 3-methyl-D-glucose or 2-deoxy-D-glucose [cf. EC 2.7.1.62 (phosphoramidate—hexose phosphotransferase), EC 2.7.1.79 (diphosphate—glycerol phosphotransferase) and EC 3.9.1.1 (phosphoamidase)].

References:

1.	Anchors, J.M. and Karnovsky, N.L. Purification of cerebral glucose-6-phosphatase. An enzyme involved in sleep. J. Biol. Chem. 250 (1975) 6408–6416. [PMID: 169241]
2.	Colilla, W., Jorgenson, R.A. and Nordlie, R.C. Mammalian carbamyl phosphate : glucose phosphotransferase and glucose-6-phosphate phosphohydrolase: extended tissue distribution. Biochim. Biophys. Acta 377 (1975) 117. [PMID: 164220]
3.	Nordlie, R.C. Glucose-6-phosphatase, hydrolytic and synthetic activities. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 4, Academic Press, New York, 1971, pp. 543–610.
4.	Nordlie, R.C. Metabolic regulation by multifunctional glucose-6-phosphatase. Curr. Top. Cell. Regul. 8 (1974) 33. [PMID: 4370737]

[EC 3.1.3.9 created 1961]

3.1.3.10

Accepted name:

glucose-1-phosphatase

Reaction:

α-D-glucose 1-phosphate + H₂O = D-glucose + phosphate

Systematic name:

α-D-glucose-1-phosphate phosphohydrolase

Comments:

Also acts, more slowly, on D-galactose 1-phosphate.

References:

1.	Faulkner, P. A hexose-1-phosphatase in silkworm blood. Biochem. J. 60 (1955) 590–596. [PMID: 13249953]
2.	Turner, D.H. and Turner, J.F. The hydrolysis of glucose monophosphates by a phosphatase preparation from pea seeds. Biochem. J. 74 (1960) 486–491. [PMID: 13839934]

[EC 3.1.3.10 created 1961]

3.1.3.11

Accepted name:

fructose-bisphosphatase

Reaction:

D-fructose 1,6-bisphosphate + H₂O = D-fructose 6-phosphate + phosphate

Other name(s):

hexose diphosphatase; FBPase; fructose 1,6-diphosphatase; fructose 1,6-diphosphate phosphatase; D-fructose 1,6-diphosphatase; fructose 1,6-bisphosphatase; fructose diphosphatase; fructose diphosphate phosphatase; fructose bisphosphate phosphatase; fructose 1,6-bisphosphate 1-phosphatase; fructose 1,6-bisphosphate phosphatase; hexose bisphosphatase; D-fructose-1,6-bisphosphate phosphatase

Systematic name:

D-fructose-1,6-bisphosphate 1-phosphohydrolase

Comments:

The animal enzyme also acts on sedoheptulose 1,7-bisphosphate.

References:

1.	El-Badry, A.M. Hexosediphosphatase from spinach chloroplasts. Purification, crystallization and some properties. Biochim. Biophys. Acta 333 (1974) 366–377. [PMID: 19400047]
2.	Gomori, G. Hexosediphosphatase. J. Biol. Chem. 148 (1943) 139–149.
3.	Mokrash, L.C. and McGilvery, R.N. Purification and properties of fructose-1,6-diphosphatase. J. Biol. Chem. 221 (1956) 909–917. [PMID: 13357486]
4.	Pontremoli, S., Traniello, S., Luppis, B. and Wood, W.A. Fructose diphosphatase from rabbit liver. I. Purification and properties. J. Biol. Chem. 240 (1965) 3459–3463. [PMID: 4284291]

[EC 3.1.3.11 created 1961, modified 1976]

3.1.3.12

Accepted name:

trehalose-phosphatase

Reaction:

α,α-trehalose 6-phosphate + H₂O = α,α-trehalose + phosphate

Other name(s):

trehalose 6-phosphatase; trehalose 6-phosphate phosphatase; trehalose-6-phosphate phosphohydrolase

Systematic name:

α,α-trehalose-6-phosphate phosphohydrolase

References:

1.	Cabib, E. and Leloir, L.F. The biosynthesis of trehalose phosphate. J. Biol. Chem. 231 (1958) 259–275. [PMID: 13538966]
2.	Candy, D.J. and Kilby, B.A. The biosynthesis of trehalose in the locust fat body. Biochem. J. 78 (1961) 531–536. [PMID: 13690400]

[EC 3.1.3.12 created 1961]

3.1.3.13

Deleted entry:

bisphosphoglycerate phosphatase. Recent studies have shown that this is a partial activity of EC 5.4.2.11, phosphoglycerate mutase (2,3-diphosphoglycerate-dependent)

[EC 3.1.3.13 created 1961, deleted 2016]

3.1.3.14

Accepted name:

methylphosphothioglycerate phosphatase

Reaction:

S-methyl-3-phospho-1-thio-D-glycerate + H₂O = S-methyl-1-thio-D-glycerate + phosphate

Other name(s):

methylthiophosphoglycerate phosphatase

Systematic name:

S-methyl-3-phospho-1-thio-D-glycerate phosphohydrolase

References:

1.	Black, S. and Wright, N.G. Enzymatic formation of glyceryl and phosphoglyceryl methylthiol esters. J. Biol. Chem. 221 (1956) 171–180. [PMID: 13345808]

[EC 3.1.3.14 created 1961]

3.1.3.15

Accepted name:

histidinol-phosphatase

Reaction:

L-histidinol phosphate + H₂O = L-histidinol + phosphate

Other name(s):

histidinol phosphate phosphatase; L-histidinol phosphate phosphatase; histidinolphosphate phosphatase; HPpase; histidinolphosphatase

Systematic name:

L-histidinol-phosphate phosphohydrolase

References:

1.	Ames, B.N. The biosynthesis of histidine; L-histidinol phosphate phosphatase. J. Biol. Chem. 226 (1957) 583–593. [PMID: 13438843]

[EC 3.1.3.15 created 1961]

3.1.3.16

Accepted name:

protein-serine/threonine phosphatase

Reaction:

[a protein]-serine/threonine phosphate + H₂O = [a protein]-serine/threonine + phosphate

Other name(s):

phosphoprotein phosphatase (ambiguous); protein phosphatase-1; protein phosphatase-2A; protein phosphatase-2B; protein phosphatase-2C; protein D phosphatase; phosphospectrin phosphatase; casein phosphatase; Aspergillus awamori acid protein phosphatase; calcineurin; phosphatase 2A; phosphatase 2B; phosphatase II; phosphatase IB; phosphatase C-II; polycation modulated (PCM-) phosphatase; phosphopyruvate dehydrogenase phosphatase; phosphatase SP; branched-chain α-keto acid dehydrogenase phosphatase; BCKDH phosphatase; 3-hydroxy 3-methylglutaryl coenzymeA reductase phosphatase; HMG-CoA reductase phosphatase; phosphatase H-II; phosphatase III; phosphatase I; protein phosphatase; phosphatase IV; phosphoprotein phosphohydrolase

Systematic name:

protein-serine/threonine-phosphate phosphohydrolase

Comments:

A group of enzymes removing the serine- or threonine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes that have been phosphorylated under the action of a kinase (cf. EC 3.1.3.48 protein-tyrosine-phosphatase). The spleen enzyme also acts on phenolic phosphates and phosphamides (cf. EC 3.9.1.1, phosphoamidase).

References:

1.	Deutscher, J., Kessler, U. and Hengstenberg, W. Streptococcal phosphoenolpyruvate: sugar phosphotransferase system: purification and characterization of a phosphoprotein phosphatase which hydrolyzes the phosphoryl bond in seryl-phosphorylated histidine-containing protein. J. Bacteriol. 163 (1985) 1203–1209. [PMID: 2993239]
2.	Ingebritsen, T.S. and Cohen, P. The protein phosphatases involved in cellular regulation. 1. Classification and substrate specificities. Eur. J. Biochem. 132 (1983) 255–261. [PMID: 6301824]
3.	Sundarajan, T.A. and Sarma, P.S. Substrate specificity of phosphoprotein phosphatase from spleen. Biochem. J. 71 (1959) 537–544. [PMID: 13638262]
4.	Tonks, N.K. and Cohen, P. The protein phosphatases involved in cellular regulation. Identification of the inhibitor-2 phosphatases in rabbit skeletal muscle. Eur. J. Biochem. 145 (1984) 65–70. [PMID: 6092084]

[EC 3.1.3.16 created 1961, modified 1989, modified 2013]

3.1.3.17

Accepted name:

[phosphorylase] phosphatase

Reaction:

[phosphorylase a] + 4 H₂O = 2 [phosphorylase b] + 4 phosphate

Other name(s):

PR-enzyme; phosphorylase a phosphatase; glycogen phosphorylase phosphatase; protein phosphatase C; type 1 protein phosphatase

Systematic name:

[phosphorylase a] phosphohydrolase

References:

1.	Brandt, H., Capulong, Z.L. and Lee, E.Y.C. Purification and properties of rabbit liver phosphorylase phosphatase. J. Biol. Chem. 250 (1975) 8038–8044. [PMID: 240850]
2.	Graves, D.J., Fischer, E.H. and Krebs, E.G. Specificity studies on muscle phosphorylase phosphatase. J. Biol. Chem. 235 (1960) 805–809. [PMID: 13829077]
3.	Rall, T.W., Wosilait, W.D. and Sutherland, E.W. The interconversion of phosphorylase a and phosphorylase b from dog heart muscle. Biochim. Biophys. Acta 20 (1956) 69–76. [PMID: 13315351]

[EC 3.1.3.17 created 1961]

3.1.3.18

Accepted name:

phosphoglycolate phosphatase

Reaction:

2-phosphoglycolate + H₂O = glycolate + phosphate

Other name(s):

phosphoglycolate hydrolase; 2-phosphoglycolate phosphatase; P-glycolate phosphatase; phosphoglycollate phosphatase

Systematic name:

2-phosphoglycolate phosphohydrolase

References:

1.	Christeller, J.T. and Tolbert, N.E. Phosphoglycolate phosphatase. Purification and properties. J. Biol. Chem. 253 (1978) 1780–1785. [PMID: 204630]

[EC 3.1.3.18 created 1965]

3.1.3.19

Accepted name:

glycerol-2-phosphatase

Reaction:

glycerol 2-phosphate + H₂O = glycerol + phosphate

Other name(s):

β-glycerophosphatase; β-glycerophosphate phosphatase; 2-glycerophosphatase

Systematic name:

glycerol-2-phosphate phosphohydrolase

References:

1.	Schmidt, G. Nonspecific acid phosphomonoesterases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 5, Academic Press, New York, 1961, pp. 37–47.
2.	Tsuboi, K.K., Wiener, G. and Hudson, P.B. Acid phosphatase. VII. Yeast phosphomonoesterase; isolation procedure and stability characteristics. J. Biol. Chem. 224 (1957) 621–635. [PMID: 13405892]

[EC 3.1.3.19 created 1965]

3.1.3.20

Accepted name:

phosphoglycerate phosphatase

Reaction:

D-glycerate 2-phosphate + H₂O = D-glycerate + phosphate

Other name(s):

D-2-phosphoglycerate phosphatase; glycerophosphate phosphatase

Systematic name:

D-glycerate-2-phosphate phosphohydrolase

References:

1.	Fallon, H.J. and Byrne, W.L. 2-Phosphoglyceric acid phosphatase: identification and properties of the beef-liver enzyme. Biochim. Biophys. Acta 105 (1965) 43–53. [PMID: 4284998]

[EC 3.1.3.20 created 1972]

3.1.3.21

Accepted name:

glycerol-1-phosphatase

Reaction:

glycerol 1-phosphate + H₂O = glycerol + phosphate

Other name(s):

α-glycerophosphatase; α-glycerol phosphatase; glycerol 3-phosphatase; glycerol-3-phosphate phosphatase; glycerol 3-phosphate phosphohydrolase

Systematic name:

glycerol-1-phosphate phosphohydrolase

Comments:

The Dunaliella enzyme acts more rapidly on sn-glycerol 1-phosphate than on the 3-phosphate. The enzyme from yeast also acts on propane-1,2-diol 1-phosphate, but not on a variety of other phosphate esters.

References:

1.	Sussman, I. and Avron, M. Characterization and partial purification of DL-glycerol-1-phosphatase from Dunaliella salina. Biochim. Biophys. Acta 661 (1981) 199–204.

[EC 3.1.3.21 created 1972, modified 1986]

3.1.3.22

Accepted name:

mannitol-1-phosphatase

Reaction:

D-mannitol 1-phosphate + H₂O = D-mannitol + phosphate

Other name(s):

mannitol-1-phosphate phosphatase

Systematic name:

D-mannitol-1-phosphate phosphohydrolase

References:

1.	Rumpho, M.E., Edwards, G.E. and Loescher, W.H. A pathway for photosynthetic carbon flow to mannitol in celery leaves. Activity and localization of key enzymes. Plant Physiol. 73 (1983) 869–873. [PMID: 16663332]
2.	Yamada, H., Okamoto, K., Kodama, K., Noguchi, F. and Tanaka, S. Enzymatic studies on mannitol formation by Piricularia oryzae. J. Biochem. (Tokyo) 49 (1961) 404–410. [PMID: 13787089]

[EC 3.1.3.22 created 1972]

3.1.3.23

Accepted name:

sugar-phosphatase

Reaction:

sugar phosphate + H₂O = sugar + phosphate

Systematic name:

sugar-phosphate phosphohydrolase

Comments:

Has a wide specificity, acting on aldohexose 1-phosphates, ketohexose 1-phosphates, aldohexose 6-phosphates, ketohexose 6-phosphates, both phosphate ester bonds of fructose 1,6-bisphosphate, phosphoric esters of disaccharides, and on pentose and triose phosphates, but at a slower rate.

References:

1.	Lee, Y.-P., Sowokinos, J.R. and Erwin, M.J. Sugar phosphate phosphohydrolase. I. Substrate specificity, intracellular localization, and purification from Neisseria meningitidis. J. Biol. Chem. 242 (1967) 2264–2271. [PMID: 4290224]

[EC 3.1.3.23 created 1972]

3.1.3.24

Accepted name:

sucrose-phosphate phosphatase

Reaction:

sucrose 6^F-phosphate + H₂O = sucrose + phosphate

Other name(s):

sucrose 6-phosphate hydrolase; sucrose-phosphate hydrolase; sucrose-phosphate phosphohydrolase; sucrose-6-phosphatase; sucrose phosphatase; sucrose-6-phosphate phosphatase; SPP

Systematic name:

sucrose-6^F-phosphate phosphohydrolase

Comments:

Requires Mg²⁺ for maximal activity [2]. This is the final step in the sucrose-biosynthesis pathway. The enzyme is highly specific for sucrose 6-phosphate, with fructose 6-phosphate unable to act as a substrate [2]. Belongs in the haloacid dehydrogenase (HAD) superfamily. The F of sucrose 6^F-phosphate is used to indicate that the fructose residue of sucrose carries the substituent.

References:

1.	Hawker, J.S. and Hatch, M.D. A specific sucrose phosphatase from plant tissues. Biochem. J. 99 (1966) 102–107. [PMID: 4290548]
2.	Lunn, J.E., Ashton, A.R., Hatch, M.D. and Heldt, H.W. Purification, molecular cloning, and sequence analysis of sucrose-6^F-phosphate phosphohydrolase from plants. Proc. Natl. Acad. Sci. USA 97 (2000) 12914–12919. [PMID: 11050182]
3.	Lunn, J.E. and MacRae, E. New complexities in the synthesis of sucrose. Curr. Opin. Plant Biol. 6 (2003) 208–214. [PMID: 12753969]
4.	Fieulaine, S., Lunn, J.E., Borel, F. and Ferrer, J.L. The structure of a cyanobacterial sucrose-phosphatase reveals the sugar tongs that release free sucrose in the cell. Plant Cell 17 (2005) 2049–2058. [PMID: 15937230]

[EC 3.1.3.24 created 1972, modified 2008]

3.1.3.25

Accepted name:

inositol-phosphate phosphatase

Reaction:

myo-inositol phosphate + H₂O = myo-inositol + phosphate

Other name(s):

myo-inositol-1(or 4)-monophosphatase; inositol 1-phosphatase; L-myo-inositol-1-phosphate phosphatase; myo-inositol 1-phosphatase; inositol phosphatase; inositol monophosphate phosphatase; inositol-1(or 4)-monophosphatase; myo-inositol-1(or 4)-phosphate phosphohydrolase; myo-inositol monophosphatase; myo-inositol-1-phosphatase

Systematic name:

myo-inositol-phosphate phosphohydrolase

Comments:

Acts on five of the six isomers of myo-inositol phosphate, all except myo-inositol 2-phosphate, but does not act on myo-inositol bearing more than one phosphate group. It also acts on adenosine 2′-phosphate (but not the 3′- or 5′- phosphates), sn-glycerol 3-phosphate and glycerol 2-phosphate. Two isoforms are known [4].

References:

1.	Eisenberg, F., Jr. D-Myoinositol 1-phosphate as product of cyclization of glucose 6-phosphate and substrate for a specific phosphatase in rat testis. J. Biol. Chem. 242 (1967) 1375–1382. [PMID: 4290245]
2.	Gee, N.S., Ragan, C.I., Watling, K.J., Aspley, S., Jackson, R.G., Reid, G.G., Gani, D. and Shute, J.K. The purification and properties of myo-inositol monophosphatase from bovine brain. Biochem. J. 249 (1988) 883–889. [PMID: 2833231]
3.	Hallcher, L.M. and Sherman, W.R. The effects of lithium ion and other agents on the activity of myo-inositol-1-phosphatase from bovine brain. J. Biol. Chem. 255 (1980) 10896–10901. [PMID: 6253491]
4.	Yoshikawa, T., Turner, G., Esterling, L.E., Sanders, A.R. and Detera-Wadleigh, S.D. A novel human myo-inositol monophosphatase gene, IMP.18p, maps to a susceptibility region for bipolar disorder. Mol. Psychiatry 2 (1997) 393–397. [PMID: 9322233]
5.	Woscholski, R. and Parker, P.J. Inositol phosphatases: constructive destruction of phosphoinositides and inositol phosphates. In: Cockcroft, S. (Ed.), Biology of Phosphoinositides, Biology of Phosphoinositides, Oxford, 2000, pp. 320–338.
6.	Ackermann, K.E., Gish, B.G., Honchar, M.P. and Sherman, W.R. Evidence that inositol 1-phosphate in brain of lithium-treated rats results mainly from phosphatidylinositol metabolism. Biochem. J. 242 (1987) 517–524. [PMID: 3036092]

[EC 3.1.3.25 created 1972, modified 1990, modified 2002, modified 2004]

3.1.3.26

Accepted name:

4-phytase

Reaction:

myo-inositol hexakisphosphate + H₂O = 1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate

Other name(s):

6-phytase (name based on 1L-numbering system and not 1D-numbering); phytase; phytate 6-phosphatase; myo-inositol-hexakisphosphate 6-phosphohydrolase (name based on 1L-numbering system and not 1D-numbering)

Systematic name:

myo-inositol-hexakisphosphate 4-phosphohydrolase

References:

1.	Johnson, L.F. and Tate, M.E. The structure of myo-inositol pentaphosphates. Ann. N.Y. Acad. Sci. 165 (1969) 526–532. [PMID: 4310376]
2.	Tomlinson, R.V. and Ballou, C.E. Myoinositol polyphosphate intermediates in the dephosphorylation of phytic acid by phytase. Biochemistry 1 (1962) 166–171. [PMID: 13921788]
3.	Lim, P.E. and Tate, M.E. The phytases. II. Properties of phytase fractions F1 and F2 from wheat bran and the myo-inositol phosphates produced by fraction F2. Biochim. Biophys. Acta 302 (1973) 316–328. [PMID: 4349266]
4.	Cosgrove, D.J. Inositol Phosphates: Their Chemistry, Biochemistry, and Physiology, Elsevier, Amsterdam, 1980.

[EC 3.1.3.26 created 1972, modified 1976, modified 2002]

3.1.3.27

Accepted name:

phosphatidylglycerophosphatase

Reaction:

phosphatidylglycerophosphate + H₂O = phosphatidylglycerol + phosphate

Other name(s):

phosphatidylglycerol phosphate phosphatase; phosphatidylglycerol phosphatase; PGP phosphatase

Systematic name:

phosphatidylglycerophosphate phosphohydrolase

References:

1.	Chang, Y.Y. and Kennedy, E.P. Phosphatidyl glycerophosphate phosphatase. J. Lipid Res. 8 (1967) 456–462. [PMID: 4292860]

[EC 3.1.3.27 created 1972]

3.1.3.28

Accepted name:

ADP-phosphoglycerate phosphatase

Reaction:

3-(ADP)-2-phosphoglycerate + H₂O = 3-(ADP)-glycerate + phosphate

Other name(s):

adenosine diphosphate phosphoglycerate phosphatase

Systematic name:

3-(ADP)-2-phosphoglycerate phosphohydrolase

Comments:

Also acts on 2,3-bisphosphoglycerate.

References:

1.	Zancan, G.T., Recondo, E.F. and Leloir, L.F. Enzymic dephosphorylation of adenosine diphosphate phosphoglyceric acid. Biochim. Biophys. Acta 92 (1964) 125–131. [PMID: 14243760]

[EC 3.1.3.28 created 1972]

3.1.3.29

Accepted name:

N-acylneuraminate-9-phosphatase

Reaction:

N-acylneuraminate 9-phosphate + H₂O = N-acylneuraminate + phosphate

Other name(s):

acylneuraminate 9-phosphatase; N-acylneuraminic acid 9-phosphate phosphatase; N-acylneuraminic (sialic) acid 9-phosphatase

Systematic name:

N-acylneuraminate-9-phosphate phosphohydrolase

References:

1.	Jourdian, G.W., Swanson, A., Watson, D. and Roseman, S. N-Acetylneuraminic (sialic) acid 9-phosphatase. Methods Enzymol. 8 (1966) 205–208.

[EC 3.1.3.29 created 1972]

3.1.3.30

Deleted entry:

3′-phosphoadenylylsulfate 3′-phosphatase. The activity may be that of an acid phosphatase.

[EC 3.1.3.30 created 1972, deleted 1992]

3.1.3.31

Deleted entry:

nucleotidase. The activity may be that of an acid phosphatase.

[EC 3.1.3.31 created 1972 (EC 3.1.3.30 created 1972, incorporated 1992), deleted 2020]

3.1.3.32

Accepted name:

polynucleotide 3′-phosphatase

Reaction:

a 3′-phosphopolynucleotide + H₂O = a polynucleotide + phosphate

Other name(s):

2′(3′)-polynucleotidase; DNA 3′-phosphatase; deoxyribonucleate 3′-phosphatase; 5′-polynucleotidekinase 3′-phosphatase

Systematic name:

polynucleotide 3′-phosphohydrolase

Comments:

Also hydrolyses nucleoside 2′-, 3′- and 5′-monophosphates, but only 2′- and 3′-phosphopolynucleotides.

References:

1.	Becker, A. and Hurwitz, J. The enzymatic cleavage of phosphate termini from polynucleotides. J. Biol. Chem. 242 (1967) 936–950. [PMID: 4289819]

[EC 3.1.3.32 created 1972]

3.1.3.33

Accepted name:

polynucleotide 5′-phosphatase

Reaction:

a 5′-phosphopolynucleotide + H₂O = a polynucleotide + phosphate

Other name(s):

5′-polynucleotidase

Systematic name:

polynucleotide 5′-phosphohydrolase

Comments:

Does not act on nucleoside monophosphates. Induced in Escherichia coli by T-even phages.

References:

1.	Becker, A. and Hurwitz, J. The enzymatic cleavage of phosphate termini from polynucleotides. J. Biol. Chem. 242 (1967) 936–950. [PMID: 4289819]

[EC 3.1.3.33 created 1972]

3.1.3.34

Accepted name:

deoxynucleotide 3′-phosphatase

Reaction:

a 2′-deoxyribonucleoside 3′-phosphate + H₂O = a 2′-deoxyribonucleoside + phosphate

Other name(s):

3′-deoxynucleotidase; 3′-deoxyribonucleotidase

Systematic name:

2′-deoxyribonucleotide 3′-phosphohydrolase

Comments:

Also catalyses the selective removal of 3′-phosphate groups from DNA and oligodeoxyribonucleotides. Induced in Escherichia coli by T-even phages.

References:

1.	Becker, A. and Hurwitz, J. The enzymatic cleavage of phosphate termini from polynucleotides. J. Biol. Chem. 242 (1967) 936–950. [PMID: 4289819]

[EC 3.1.3.34 created 1972]

3.1.3.35

Accepted name:

thymidylate 5′-phosphatase

Reaction:

thymidylate + H₂O = thymidine + phosphate

Other name(s):

thymidylate 5′-nucleotidase; deoxythymidylate 5′-nucleotidase; thymidylate nucleotidase; deoxythymidylic 5′-nucleotidase; deoxythymidylate phosphohydrolase; dTMPase

Systematic name:

thymidylate 5′-phosphohydrolase

Comments:

Acts on 5-methyl-dCMP and on TMP, but more slowly than on dTMP.

References:

1.	Aposhian, H.V. and Tremblay, G.Y. Deoxythymidylate 5′-nucleotidase. Purification and properties of an enzyme found after infection of Bacillus subtilis with phage SP₅C. J. Biol. Chem. 241 (1966) 5095–5101. [PMID: 4958986]

[EC 3.1.3.35 created 1972]

3.1.3.36

Accepted name:

phosphoinositide 5-phosphatase

Reaction:

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H₂O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate

Glossary:

1-phosphatidyl-1D-myo-inositol 4-phosphate = PtdIns4P
1-phosphatidyl-1D-myo-inositol 1,4-bisphosphate = PtdIns(1,4)P₂
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = PtdIns(4,5)P₂
1-phosphatidyl-1D-myo-inositol 1,3,4-trisphosphate = PtdIns(1,3,4)P₃
1-phosphatidyl-1D-myo-inositol 1,4,5-trisphosphate = PtdIns(1,4,5)P₃
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate = PtdIns(3,4,5)P₃
1-phosphatidyl-1D-myo-inositol 1,3,4,5-tetrakisphosphate = PtdIns(1,3,4,5)P₄

Other name(s):

type II inositol polyphosphate 5-phosphatase; triphosphoinositide phosphatase; IP₃ phosphatase; PtdIns(4,5)P₂ phosphatase; triphosphoinositide phosphomonoesterase; diphosphoinositide phosphatase; inositol 1,4,5-triphosphate 5-phosphomonoesterase; inositol triphosphate 5-phosphomonoesterase; phosphatidylinositol-bisphosphatase; phosphatidyl-myo-inositol-4,5-bisphosphate phosphatase; phosphatidylinositol 4,5-bisphosphate phosphatase; polyphosphoinositol lipid 5-phosphatase; phosphatidyl-inositol-bisphosphate phosphatase

Systematic name:

phosphatidyl-myo-inositol-4,5-bisphosphate 4-phosphohydrolase

Comments:

These enzymes can also remove the 5-phosphate from Ins(1,4,5)P₃ and/or Ins(1,3,4,5)P₄. They are a diverse family of enzymes, with differing abilities to catalyse two or more of the four reactions listed. They are thought to use inositol lipids rather than inositol phosphates as substrates in vivo. All of them can use either or both of PtdIns(4,5)P₂ and PtdIns(3,4,5)P₃ as substrates; this is the main property that distinguishes them from EC 3.1.3.56, inositol-polyphosphate 5-phosphatase.

References:

1.	Dawson, R.M.C. and Thompson, W. The triphosphoinositide phosphomonoesterase of brain tissue. Biochem. J. 91 (1964) 244–250. [PMID: 4284485]
2.	Roach, P.D. and Palmer, F.B.S. Human erythrocyte cytosol phosphatidyl-inositol-bisphosphate phosphatase. Biochim. Biophys. Acta 661 (1981) 323–333. [PMID: 6271223]
3.	Woscholski, R. and Parker, P.J. Inositol phosphatases: constructive destruction of phosphoinositides and inositol phosphates. In: Cockcroft, S. (Ed.), Biology of Phosphoinositides, Biology of Phosphoinositides, Oxford, 2000, pp. 320–338.

[EC 3.1.3.36 created 1972, modified 2002]

3.1.3.37

Accepted name:

sedoheptulose-bisphosphatase

Reaction:

sedoheptulose 1,7-bisphosphate + H₂O = sedoheptulose 7-phosphate + phosphate

Other name(s):

SBPase; sedoheptulose 1,7-diphospate phosphatase; sedoheptulose 1,7-diphosphatase; sedoheptulose diphosphatase; sedoheptulose bisphosphatase; sedoheptulose 1,7-bisphosphatase

Systematic name:

sedoheptulose-1,7-bisphosphate 1-phosphohydrolase

References:

1.	Racker, E. Sedoheptulose-1,7-diphosphatase from yeast. Methods Enzymol. 5 (1962) 270–272.
2.	Traniello, S., Calcagno, M. and Pontremoli, S. Fructose 1,6-diphosphatase and sedoheptulose 1,7-diphosphatase from Candida utilis: purification and properties. Arch. Biochem. Biophys. 146 (1971) 603–610. [PMID: 4329855]

[EC 3.1.3.37 created 1976]

3.1.3.38

Accepted name:

3-phosphoglycerate phosphatase

Reaction:

D-glycerate 3-phosphate + H₂O = D-glycerate + phosphate

Other name(s):

D-3-Phosphoglycerate phosphatase; 3-PGA phosphatase

Systematic name:

D-glycerate-3-phosphate phosphohydrolase

Comments:

Wide specificity, but 3-phosphoglycerate is the best substrate.

References:

1.	Randall, D.D. and Tolbert, N.E. 3-Phosphoglycerate phosphatase in plants. I. Isolation and characterization from sugarcane leaves. J. Biol. Chem. 246 (1971) 5510–5517. [PMID: 10970181]

[EC 3.1.3.38 created 1976]

3.1.3.39

Accepted name:

streptomycin-6-phosphatase

Reaction:

streptomycin 6-phosphate + H₂O = streptomycin + phosphate

Other name(s):

streptomycin 6-phosphate phosphatase; streptomycin 6-phosphate phosphohydrolase; streptomycin-6-P phosphohydrolase

Systematic name:

streptomycin-6-phosphate phosphohydrolase

Comments:

Also acts on dihydrostreptomycin 3′α,6-bisphosphate and streptidine 6-phosphate.

References:

1.	Walker, J.B. and Skorvaga, M. Streptomycin biosynthesis and metabolism. Phosphate transfer from dihydrostreptomycin 6-phosphate to inosamines, streptamine, and 2-deoxystreptamine. J. Biol. Chem. 248 (1973) 2441–2446. [PMID: 4121457]
2.	Walker, M.S. and Walker, J.B. Streptomycin biosynthesis. Separation and substrate specificities of phosphatases acting on guanidinodeoxy-scyllo-inositol phosphate and streptomycin-(streptidino)phosphate. J. Biol. Chem. 246 (1971) 7034–7040. [PMID: 4331203]

[EC 3.1.3.39 created 1976]

3.1.3.40

Accepted name:

guanidinodeoxy-scyllo-inositol-4-phosphatase

Reaction:

1-guanidino-1-deoxy-scyllo-inositol 4-phosphate + H₂O = 1-guanidino-1-deoxy-scyllo-inositol + phosphate

Other name(s):

1-guanidino-scyllo-inositol 4-phosphatase; 1-guanidino-1-deoxy-scyllo-inositol-4-P phosphohydrolase

Systematic name:

1-guanidino-1-deoxy-scyllo-inositol-4-phosphate 4-phosphohydrolase

References:

1.	Walker, M.S. and Walker, J.B. Streptomycin biosynthesis. Separation and substrate specificities of phosphatases acting on guanidinodeoxy-scyllo-inositol phosphate and streptomycin-(streptidino)phosphate. J. Biol. Chem. 246 (1971) 7034–7040. [PMID: 4331203]

[EC 3.1.3.40 created 1976]

3.1.3.41

Accepted name:

4-nitrophenylphosphatase

Reaction:

4-nitrophenyl phosphate + H₂O = 4-nitrophenol + phosphate

Other name(s):

nitrophenyl phosphatase; p-nitrophenylphosphatase; para-nitrophenyl phosphatase; K-pNPPase; NPPase; PNPPase; Ecto-p-nitrophenyl phosphatase; p-nitrophenylphosphate phosphohydrolase

Systematic name:

4-nitrophenylphosphate phosphohydrolase

Comments:

A number of other substances, including phenyl phosphate, 4-nitrophenyl sulfate, acetyl phosphate and glycerol phosphate, are not substrates.

References:

1.	Attias, J. and Bonnet, J.L. A specific alkaline p-nitrophenylphosphatase activity from baker's yeast. Biochim. Biophys. Acta 268 (1972) 422–430. [PMID: 4554643]
2.	Attias, J. and Durand, H. Further characterization of a specific p-nitrophenylphosphatase from baker's yeast. Biochim. Biophys. Acta 321 (1973) 561–568. [PMID: 4357666]

[EC 3.1.3.41 created 1976]

3.1.3.42

Accepted name:

[glycogen-synthase-D] phosphatase

Reaction:

[glycogen-synthase D] + H₂O = [glycogen-synthase I] + phosphate

Other name(s):

uridine diphosphoglucose-glycogen glucosyltransferase phosphatase; UDP-glycogen glucosyltransferase phosphatase; UDPglucose-glycogen glucosyltransferase phosphatase; glycogen glucosyltransferase phosphatase; glycogen synthetase phosphatase; glycogen synthase phosphatase; glycogen synthase D phosphatase; Mg²⁺ dependent glycogen synthase phosphatase; phosphatase type 2°C

Systematic name:

[UDP-glucose:glycogen 4-α-D-glucosyltransferase-D] phosphohydrolase

Comments:

The product is EC 2.4.1.11 glycogen(starch) synthase.

References:

1.	Abe, N. and Tsuiki, S. Studies on glycogen synthase D phosphatase of rat liver - multiple nature. Biochim. Biophys. Acta 350 (1974) 383–391. [PMID: 4367978]

[EC 3.1.3.42 created 1976]

3.1.3.43

Accepted name:

[pyruvate dehydrogenase (acetyl-transferring)]-phosphatase

Reaction:

[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H₂O = [pyruvate dehydrogenase (acetyl-transferring)] + phosphate

Glossary:

lipoyl group

Other name(s):

pyruvate dehydrogenase phosphatase; phosphopyruvate dehydrogenase phosphatase; [pyruvate dehydrogenase (lipoamide)]-phosphatase; [pyruvate dehydrogenase (lipoamide)]-phosphate phosphohydrolase

Systematic name:

[pyruvate dehydrogenase (acetyl-transferring)]-phosphate phosphohydrolase

Comments:

A mitochondrial enzyme associated with EC 1.2.4.1 pyruvate dehydrogenase (acetyl-transferring), in the pyruvate dehydrogenase complex.

References:

1.	Linn, T.C., Pelley, J.W., Petit, F.H., Hucho, F., Randall, D.D. and Reed, L.J. α-Keto acid dehydrogenase complexes. XV. Purification and properties of the component enzymes of the pyruvate dehydrogenase complexes from bovine kidney and heart. Arch. Biochem. Biophys. 148 (1972) 327–342. [PMID: 4401694]
2.	Reed, L.J., Damuni, Z. and Merryfield, M.L. Regulation of mammalian pyruvate and branched-chain α-keto acid dehydrogenase complexes by phosphorylation-dephosphorylation. Curr. Top. Cell. Regul. 27 (1985) 41–49. [PMID: 3004826]

[EC 3.1.3.43 created 1978]

3.1.3.44

Accepted name:

[acetyl-CoA carboxylase]-phosphatase

Reaction:

[acetyl-CoA carboxylase] phosphate + H₂O = [acetyl-CoA carboxylase] + phosphate

Systematic name:

[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]-phosphate phosphohydrolase

Comments:

Simultaneously dephosphorylates and activates EC 6.4.1.2 acetyl-CoA carboxylase. Acts similarly on EC 1.1.1.88 (hydroxymethylglutaryl-CoA reductase), EC 2.4.1.1 (phosphorylase), EC 2.4.1.11 [glycogen(starch) synthase], and dephosphorylates phosphoprotamine and 4-nitrophenyl phosphate. Not identical to EC 3.1.3.17 ([phosphorylase] phosphatase ) or EC 3.1.3.43 {[pyruvate dehydrogenase (acetyl-transferring)]-phosphatase}.

References:

1.	Krakower, G.R. and Kim, K.-H. Purification and properties of acetyl-CoA carboxylase phosphatase. J. Biol. Chem. 256 (1980) 2408–2413. [PMID: 6257718]

[EC 3.1.3.44 created 1983]

3.1.3.45

Accepted name:

3-deoxy-manno-octulosonate-8-phosphatase

Reaction:

3-deoxy-D-manno-octulosonate 8-phosphate + H₂O = 3-deoxy-D-manno-octulosonate + phosphate

Systematic name:

3-deoxy-D-manno-octulosonate-8-phosphate 8-phosphohydrolase

References:

1.	Ray, P.H. and Benedict, C.D. Purification and characterization of specific 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase from Escherichia coli B. J. Bacteriol. 142 (1980) 60–68. [PMID: 6246070]

[EC 3.1.3.45 created 1983]

3.1.3.46

Accepted name:

fructose-2,6-bisphosphate 2-phosphatase

Reaction:

β-D-fructose 2,6-bisphosphate + H₂O = D-fructose 6-phosphate + phosphate

Other name(s):

fructose-2,6-bisphosphatase; D-fructose-2,6-bisphosphate 2-phosphohydrolase

Systematic name:

β-D-fructose-2,6-bisphosphate 2-phosphohydrolase

Comments:

The enzyme copurifies with EC 2.7.1.105 6-phosphofructo-2-kinase. (cf. EC 3.1.3.54 fructose-2,6-bisphosphate 6-phosphatase).

References:

1.	Van Schaftingen, E., Davies, D.R. and Hers, H.-G. Fructose-2,6-bisphosphatase from rat liver. Eur. J. Biochem. 124 (1982) 143–149. [PMID: 6282585]

[EC 3.1.3.46 created 1984]

3.1.3.47

Accepted name:

[hydroxymethylglutaryl-CoA reductase (NADPH)]-phosphatase

Reaction:

[hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate + H₂O = [hydroxymethylglutaryl-CoA reductase (NADPH)] + phosphate

Other name(s):

reductase phosphatase

Systematic name:

[hydroxymethylglutaryl-CoA reductase (NADPH)]-phosphate phosphohydrolase

Comments:

Acts on the product of the reaction catalysed by EC 2.7.11.31 [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase, simultaneously dephosphorylating and activating EC 1.1.1.34 hydroxymethylglutaryl-CoA reductase (NADPH).

References:

1.	Gil, G. and Hegardt, F.G. Some properties of purified 3-hydroxy-3-methylglutaryl coenzyme A reductase phosphatases from rat liver. Arch. Biochem. Biophys. 214 (1982) 192–198. [PMID: 6282220]
2.	Gil, G., Sitges, M. and Hegardt, F.G. Purification and properties of rat liver hydroxymethylglutaryl coenzyme A reductase phosphatases. Biochim. Biophys. Acta 663 (1981) 211–221. [PMID: 6260210]

[EC 3.1.3.47 created 1984]

3.1.3.48

Accepted name:

protein-tyrosine-phosphatase

Reaction:

[a protein]-tyrosine phosphate + H₂O = [a protein]-tyrosine + phosphate

Other name(s):

phosphotyrosine phosphatase; phosphoprotein phosphatase (phosphotyrosine); phosphotyrosine histone phosphatase; protein phosphotyrosine phosphatase; tyrosylprotein phosphatase; phosphotyrosine protein phosphatase; phosphotyrosylprotein phosphatase; tyrosine O-phosphate phosphatase; PPT-phosphatase; PTPase; [phosphotyrosine]protein phosphatase; PTP-phosphatase

Systematic name:

protein-tyrosine-phosphate phosphohydrolase

Comments:

Dephosphorylates O-phosphotyrosine groups in phosphoproteins, such as the products of EC 2.7.10.2, non-specific protein-tyrosine kinase.

References:

1.	Foulkes, J.G., Howard, R.F. and Ziemiecki, A. Detection of a novel mammalian protein phosphatase with activity for phosphotyrosine. FEBS Lett. 130 (1981) 197–200. [PMID: 6169552]
2.	Gallis, B., Bornstein, P. and Brautigan, D.L. Tyrosylprotein kinase and phosphatase activities in membrane vesicles from normal and Rous sarcoma virus-transformed rat cells. Proc. Natl. Acad. Sci. USA 78 (1981) 6689–6693. [PMID: 6273884]

[EC 3.1.3.48 created 1984]

3.1.3.49

Accepted name:

[pyruvate kinase]-phosphatase

Reaction:

[pyruvate kinase] phosphate + H₂O = [pyruvate kinase] + phosphate

Other name(s):

pyruvate kinase phosphatase

Systematic name:

[ATP:pyruvate 2-O-phosphotransferase]-phosphate phosphohydrolase

Comments:

Simultaneously dephosphorylates and activates EC 2.7.1.40 pyruvate kinase, that has been inactivated by protein kinase.

References:

1.	Jett, M.-F., Hue, L. and Hers, H.-G. Pyruvate kinase phosphatase. FEBS Lett. 132 (1981) 183–186. [PMID: 6271587]

[EC 3.1.3.49 created 1984]

3.1.3.50

Accepted name:

sorbitol-6-phosphatase

Reaction:

sorbitol 6-phosphate + H₂O = sorbitol + phosphate

Other name(s):

sorbitol-6-phosphate phosphatase

Systematic name:

sorbitol-6-phosphate phosphohydrolase

Comments:

Acts, very slowly, on hexose 6-phosphates.

References:

1.	Grant, C.R. and ap Rees, T. Sorbitol metabolism by apple seedlings. Phytochemistry 20 (1981) 1505–1511.

[EC 3.1.3.50 created 1984]

3.1.3.51

Accepted name:

dolichyl-phosphatase

Reaction:

dolichyl phosphate + H₂O = dolichol + phosphate

Other name(s):

dolichol phosphate phosphatase; dolichol phosphatase; dolichol monophosphatase; dolichyl monophosphate phosphatase; dolichyl phosphate phosphatase; polyisoprenyl phosphate phosphatase; polyprenylphosphate phosphatase; Dol-P phosphatase

Systematic name:

dolichyl-phosphate phosphohydrolase

References:

1.	Adrian, G.S. and Keenan, R.W. A dolichyl phosphate-cleaving acid phosphatase from Tetrahymena pyriformis. Biochim. Biophys. Acta 575 (1979) 431–438. [PMID: 229909]
2.	Rip, J.W., Rupar, C.A., Chaudhary, N. and Carroll, K.K. Localization of a dolichyl phosphate phosphatase in plasma membranes of rat liver. J. Biol. Chem. 256 (1981) 1929–1934. [PMID: 6257694]
3.	Wedgwood, J.F. and Strominger, J.L. Enzymatic activities in cultured human lymphocytes that dephosphorylate dolichyl pyrophosphate and dolichyl phosphate. J. Biol. Chem. 255 (1980) 1120–1123. [PMID: 6243292]

[EC 3.1.3.51 created 1984]

3.1.3.52

Accepted name:

[3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)]-phosphatase

Reaction:

[3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)] phosphate + H₂O = [3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)] + phosphate

Glossary:

lipoyl group

Other name(s):

branched-chain oxo-acid dehydrogenase phosphatase; branched-chain 2-keto acid dehydrogenase phosphatase; branched-chain α-keto acid dehydrogenase phosphatase; BCKDH (ambiguous); [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]-phosphatase; [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]-phosphate phosphohydrolase

Systematic name:

[3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)]-phosphate phosphohydrolase

Comments:

A mitochondrial enzyme associated with the 3-methyl-2-oxobutanoate dehydrogenase complex. Simultaneously dephosphorylates and activates EC 1.2.4.4 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring), that has been inactivated by phosphorylation.

References:

1.	Fatania, H.R., Patston, P.A. and Randle, P.J. Dephosphorylation and reactivation of phosphorylated purified ox-kidney branched-chain dehydrogenase complex by co-purified phosphatase. FEBS Lett. 158 (1983) 234–238. [PMID: 6307746]
2.	Reed, L.J., Damuni, Z. and Merryfield, M.L. Regulation of mammalian pyruvate and branched-chain α-keto acid dehydrogenase complexes by phosphorylation-dephosphorylation. Curr. Top. Cell. Regul. 27 (1985) 41–49. [PMID: 3004826]

[EC 3.1.3.52 created 1986]

3.1.3.53

Accepted name:

[myosin-light-chain] phosphatase

Reaction:

[myosin light-chain] phosphate + H₂O = [myosin light-chain] + phosphate

Other name(s):

myosin light chain kinase phosphatase; myosin phosphatase; myosin phosphatase; protein phosphatase 2A; myosin-light-chain-phosphatase

Systematic name:

[myosin-light-chain]-phosphate phosphohydrolase

Comments:

The enzyme is composed of three subunits. The holoenzyme dephosphorylates myosin light chains and EC 2.7.11.18, myosin-light-chain kinase, but not myosin; the catalytic subunit acts on all three substrates.

References:

1.	Pato, M.D. and Adelstein, R.S. Purification and characterization of a multisubunit phosphatase from turkey gizzard smooth muscle. The effect of calmodulin binding to myosin light chain kinase on dephosphorylation. J. Biol. Chem. 258 (1983) 7047–7054. [PMID: 6304072]

[EC 3.1.3.53 created 1986]

3.1.3.54

Accepted name:

fructose-2,6-bisphosphate 6-phosphatase

Reaction:

β-D-fructose 2,6-bisphosphate + H₂O = β-D-fructofuranose 2-phosphate + phosphate

Other name(s):

fructose 2,6-bisphosphate-6-phosphohydrolase; fructose-2,6-bisphosphate 6-phosphohydrolase; D-fructose-2,6-bisphosphate 6-phosphohydrolase

Systematic name:

β-D-fructose-2,6-bisphosphate 6-phosphohydrolase

Comments:

cf. EC 3.1.3.46 fructose-2,6-bisphosphate 2-phosphatase.

References:

1.	Purwin, C., Laux, M. and Holzer, H. Fructose 2-phosphate, an intermediate of the dephosphorylation of fructose 2,6-bisposphate with purified yeast enzyme. Eur. J. Biochem. 164 (1986) 27–30.
2.	Purwin, C., Laux, M. and Holzer, H. Fructofuranose 2-phosphate is the product of dephosphorylation of fructose 2,6-bisphosphate. Eur. J. Biochem. 165 (1987) 543–545. [PMID: 3036508]

[EC 3.1.3.54 created 1989]

3.1.3.55

Accepted name:

caldesmon-phosphatase

Reaction:

caldesmon phosphate + H₂O = caldesmon + phosphate

Other name(s):

SMP-I; smooth muscle caldesmon phosphatase

Systematic name:

caldesmon-phosphate phosphohydrolase

Comments:

Dephosphorylation activates the calmodulin- and actin-binding ability of the protein caldesmon.

References:

1.	Ngai, P.K. and Walsh, M.P. Inhibition of smooth muscle actin-activated myosin Mg²⁺-ATPase activity by caldesmon. J. Biol. Chem. 259 (1984) 13656–13659. [PMID: 6150036]

[EC 3.1.3.55 created 1989]

3.1.3.56

Accepted name:

inositol-polyphosphate 5-phosphatase

Reaction:

(1) D-myo-inositol 1,4,5-trisphosphate + H₂O = myo-inositol 1,4-bisphosphate + phosphate
(2) 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H₂O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate

Other name(s):

type I inositol-polyphosphate phosphatase; inositol trisphosphate phosphomonoesterase; InsP₃/Ins(1,3,4,5)P₄ 5-phosphatase; inosine triphosphatase; D-myo-inositol 1,4,5-triphosphate 5-phosphatase; D-myo-inositol 1,4,5-trisphosphate 5-phosphatase; L-myo-inositol 1,4,5-trisphosphate-monoesterase; inositol phosphate 5-phosphomonoesterase; inositol-1,4,5-trisphosphate/1,3,4,5-tetrakisphosphate 5-phosphatase; Ins(1,4,5)P₃ 5-phosphatase; D-myo-inositol(1,4,5)/(1,3,4,5)-polyphosphate 5-phosphatase; inositol 1,4,5-trisphosphate phosphatase; inositol polyphosphate-5-phosphatase; myo-inositol-1,4,5-trisphosphate 5-phosphatase; inositol-1,4,5-trisphosphate 5-phosphatase

Systematic name:

1D-myo-inositol-1,4,5-trisphosphate 5-phosphohydrolase

Comments:

One mammalian isoform is known. This enzyme is distinguished from the family of enzymes classified under EC 3.1.3.36, phosphoinositide 5-phosphatase, by its inability to dephosphorylate inositol lipids.

References:

1.	Downes, C.P., Mussat, M.C. and Michell, R.H. The inositol trisphosphate phosphomonoesterase of the human erythrocyte membrane. Biochem. J. 203 (1982) 169–177. [PMID: 6285891]
2.	Erneux, C., Lemos, M., Verjans, B., Vanderhaeghen, P., Delvaux, A. and Dumont, J.E. Soluble and particulate Ins(1,4,5)P₃/Ins(1,3,4,5)P₄ 5-phosphatase in bovine brain. Eur. J. Biochem. 181 (1989) 317–322. [PMID: 2540972]
3.	Woscholski, R. and Parker, P.J. Inositol phosphatases: constructive destruction of phosphoinositides and inositol phosphates. In: Cockcroft, S. (Ed.), Biology of Phosphoinositides, Biology of Phosphoinositides, Oxford, 2000, pp. 320–338.
4.	Verjans, B., De Smedt, F., Lecocq, R., Vanweyenberg, V., Moreau, C. and Erneux, C. Cloning and expression in Escherichia coli of a dog thyroid cDNA encoding a novel inositol 1,4,5-trisphosphate 5-phosphatase. Biochem. J. 300 (1994) 85–90. [PMID: 8198557]

[EC 3.1.3.56 created 1989, modified 2002]

3.1.3.57

Accepted name:

inositol-1,4-bisphosphate 1-phosphatase

Reaction:

1D-myo-inositol 1,4-bisphosphate + H₂O = 1D-myo-inositol 4-phosphate + phosphate

Other name(s):

inositol-polyphosphate 1-phosphatase

Systematic name:

1D-myo-inositol-1,4-bisphosphate 1-phosphohydrolase

Comments:

The enzyme acts on inositol 1,4-bisphosphate and inositol 1,3,4-trisphosphate (forming inositol 3,4-bisphosphate) with similar V_max values for both substrates, but with a five-times higher affinity for the bisphosphate. Does not act on inositol 1-phosphate, inositol 1,4,5-trisphosphate or inositol 1,3,4,5-tetrakisphosphate.

References:

1.	Berridge, M.J., Dawson, R.M.C., Downes, C.P., Heslop, J.P. and Irvine, R.F. Changes in the levels of inositol phosphates after agonist-dependent hydrolysis of membrane phosphoinositides. Biochem. J. 212 (1983) 473–482. [PMID: 6309146]
2.	Connolly, T.M., Bansal, V.S., Bross, T.E., Irvine, R.F. and Majerus, P.W. The metabolism of tris- and tetraphosphates of inositol by 5-phosphomonoesterase and 3-kinase enzymes. J. Biol. Chem. 262 (1987) 2146–2149. [PMID: 3029066]
3.	Inhorn, R.C. and Majerus, P.W. Inositol polyphosphate 1-phosphatase from calf brain. Purification and inhibition by Li⁺, Ca²⁺, and Mn²⁺. J. Biol. Chem. 262 (1987) 15946–15952. [PMID: 2824473]

[EC 3.1.3.57 created 1989, modified 2002]

3.1.3.58

Accepted name:

sugar-terminal-phosphatase

Reaction:

D-glucose 6-phosphate + H₂O = D-glucose + phosphate

Other name(s):

xylitol-5-phosphatase

Systematic name:

sugar-ω-phosphate phosphohydrolase

Comments:

Acts on sugars and polyols phosphorylated on the terminal carbon, with a preference for sugars with a D-erythro-configuration, e.g. good substrates are glucose 6-phosphate, mannose 6-phosphate, 6-phosphogluconate, erythrose 4-phosphate and xylitol 5-phosphate.

References:

1.	London, J., Hausman, S.Z. and Thompson, J. Characterization of a membrane-regulated sugar phosphate phosphohydrolase from Lactobacillus casei. J. Bacteriol. 163 (1985) 951–956. [PMID: 2993253]

[EC 3.1.3.58 created 1989]

3.1.3.59

Accepted name:

alkylacetylglycerophosphatase

Reaction:

1-alkyl-2-acetyl-sn-glycero-3-phosphate + H₂O = 1-alkyl-2-acetyl-sn-glycerol + phosphate

Other name(s):

1-alkyl-2-lyso-sn-glycero-3-P:acetyl-CoA acetyltransferase; alkylacetylglycerophosphate phosphatase

Systematic name:

1-alkyl-2-acetyl-sn-glycero-3-phosphate phosphohydrolase

Comments:

Involved in the biosynthesis of thrombocyte activating factor in animal tissues.

References:

Lee, T.-C., Malone, B. and Snyder, F. A new de novo pathway for the formation of 1-alkyl-2-acetyl-sn-glycerols, precursors of platelet activating factor. Biochemical characterization of 1-alkyl-2-lyso-sn-glycero-3-P:acetyl-CoA acetyltransferase in rat spleen. J. Biol. Chem. 261 (1986) 5373–5377. [PMID: 3007498]

[EC 3.1.3.59 created 1989]

3.1.3.60

Accepted name:

phosphoenolpyruvate phosphatase

Reaction:

phosphoenolpyruvate + H₂O = pyruvate + phosphate

Other name(s):

PEP phosphatase

Systematic name:

phosphoenolpyruvate phosphohydrolase

Comments:

Also acts, but more slowly, on a wide range of other monophosphates.

References:

1.	Duff, S.M.G., Lefebvre, D.D. and Plaxton, W.C. Purification and characterization of a phosphoenolpyruvate phosphatase from Brassica nigra suspension cells. Plant Physiol. 90 (1989) 734–741. [PMID: 16666836]
2.	Malhotra, O.P. and Kayastha, A.M. Chemical inactivation and active site groups of phosphoenolpyruvate-phosphatase from germinating mung beans (Vigna radiata). Plant Sci. 65 (1989) 161–170.
3.	Malhotra, O.P. and Kayastha, A.M. Isolation and characterization of phosphoenolpyruvate phosphatase from germinating mung beans (Vigna radiata). Plant Physiol. 93 (1990) 194–200. [PMID: 16667434]

[EC 3.1.3.60 created 1992]

3.1.3.61

Deleted entry:

inositol-1,4,5-trisphosphate 1-phosphatase, as its existence has not been established

[EC 3.1.3.61 created 1992, deleted 2002]

3.1.3.62

Accepted name:

multiple inositol-polyphosphate phosphatase

Reaction:

myo-inositol hexakisphosphate + H₂O = myo-inositol pentakisphosphate (mixed isomers) + phosphate

Other name(s):

inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase; inositol 1,3,4,5-tetrakisphosphate 3-phosphomonoesterase; inositol 1,3,4,5-tetrakisphosphate-5-phosphomonoesterase; inositol tetrakisphosphate phosphomonoesterase; inositol-1,3,4,5-tetrakisphosphate 3-phosphatase; MIPP

Systematic name:

1D-myo-inositol-hexakisphosphate 5-phosphohydrolase

Comments:

This enzyme exists in two isoforms. It also acts on Ins(1,3,4,5)P₄ to yield Ins(1,4,5)P₃.

References:

1.	Cullen, P.J., Irvine, R.F., Drøbak, B.J. and Dawson, A.P. Inositol 1,3,4,5-tetrakisphosphate causes release of Ca²⁺ from permeabilized mouse lymphoma L1210 cells by its conversion into inositol 1,4,5-trisphosphate. Biochem. J. 259 (1989) 931–933. [PMID: 2786415]
2.	Craxton, A., Caffrey, J.J., Burkhart, W., Safrany, S.T. and Shears, S.B. Molecular cloning and expression of a rat hepatic multiple inositol polyphosphate phosphatase. Biochem. J. 328 (1997) 75–81. [PMID: 9359836]

[EC 3.1.3.62 created 1992, modified 2002]

3.1.3.63

Accepted name:

2-carboxy-D-arabinitol-1-phosphatase

Reaction:

2-carboxy-D-arabinitol 1-phosphate + H₂O = 2-carboxy-D-arabinitol + phosphate

Other name(s):

2-carboxyarabinitol 1-phosphatase; 2-carboxy-D-arabinitol 1-phosphate phosphohydrolase

Systematic name:

2-carboxy-D-arabinitol-1-phosphate 1-phosphohydrolase

References:

1.	Salvucci, M.E. and Holbrook, G.P. Purification and properties of 2-carboxy-D-arabinitol 1-phosphatase. Plant Physiol. 90 (1989) 679–685. [PMID: 16666827]

[EC 3.1.3.63 created 1992]

3.1.3.64

Accepted name:

phosphatidylinositol-3-phosphatase

Reaction:

1-phosphatidyl-1D-myo-inositol 3-phosphate + H₂O = 1-phosphatidyl-1D-myo-inositol + phosphate

Glossary:

inositol 1-phosphate = Ins-1-P
inositol 1,3-bisphosphate = Ins(1,3)P₂
1-phosphatidyl-1D-myo-inositol = PtdIns
1-phosphatidyl-1D-myo-inositol 3-phosphate = PtdIns3P

Other name(s):

inositol-1,3-bisphosphate 3-phosphatase; inositol 1,3-bisphosphate phosphatase; inositol-polyphosphate 3-phosphatase; D-myo-inositol-1,3-bisphosphate 3-phosphohydrolase; phosphatidyl-3-phosphate 3-phosphohydrolase

Systematic name:

1-phosphatidyl-1D-myo-inositol-3-phosphate 3-phosphohydrolase

Comments:

This enzyme still works when the 2,3-bis(acyloxy)propyl group is removed, i.e., it hydrolyses Ins(1,3)P₂ to Ins-1-P.

References:

1.	Lips, D.L. and Majerus, P.W. The discovery of a 3-phosphomonoesterase that hydrolyzes phosphatidylinositol 3-phosphate in NIH 3T3 cells. J. Biol. Chem. 264 (1989) 19911–19915. [PMID: 2555336]
2.	Caldwell, K.K., Lips, D.L., Bansal, V.S. and Majerus, P.W. Isolation and characterization of two 3-phosphatases that hydrolyze both phosphatidylinositol 3-phosphate and inositol 1,3-bisphosphate. J. Biol. Chem. 266 (1991) 18378–18386. [PMID: 1655747]

[EC 3.1.3.64 created 1992, [EC 3.1.3.65 created 1992, incorporated 2002], modified 2002]]

3.1.3.65

Deleted entry:

inositol-1,3-bisphosphate 3-phosphatase. Now included with EC 3.1.3.64, phosphatidylinositol-3-phosphatase

[EC 3.1.3.65 created 1992, deleted 2002]

3.1.3.66

Accepted name:

phosphatidylinositol-3,4-bisphosphate 4-phosphatase

Reaction:

1-phosphatidyl-myo-inositol 3,4-bisphosphate + H₂O = 1-phosphatidyl-1D-myo-inositol 3-phosphate + phosphate

Glossary:

inositol 3-phosphate = Ins-3-P
inositol 1,3-bisphosphate = Ins(1,3)P₂
inositol 3,4-bisphosphate = Ins(3,4)P₂
inositol 1,3,4-trisphosphate = Ins(1,3,4)P₃
1-phosphatidyl-1D-myo-inositol 3-phosphate = PtdIns3P
1-phosphatidyl-1D-myo-inositol 4-phosphate = PtdIns4P

Other name(s):

inositol-3,4-bisphosphate 4-phosphatase; D-myo-inositol-3,4-bisphosphate 4-phosphohydrolase; phosphoinositide 4-phosphatase; inositol polyphosphate 4-phosphatase; inositol polyphosphate 4-phosphatase type II

Systematic name:

1-phosphatidyl-1D-myo-inositol-3,4-bisphosphate 4-phosphohydrolase

Comments:

Mg²⁺-independent. This enzyme still works when the 2,3-bis(acyloxy)propyl group is removed, i.e., it hydrolyses Ins(1,3,4)P₃ to Ins(1,3)P₂. It also converts Ins(3,4)P₂ into Ins-3-P.

References:

1.	Howell, S., Barnaby, R.J., Rowe, T., Ragan, C.I. and Gee, N.S. Evidence for at least four different inositol bisphosphatases in bovine brain. Eur. J. Biochem. 183 (1989) 169–172. [PMID: 2546770]
2.	Norris, F.A., Auethavekiat, V. and Majerus, P.W. The isolation and characterization of cDNA encoding human and rat brain inositol polyphosphate 4-phosphatase. J. Biol. Chem. 270 (1995) 16128–16133. [PMID: 7608176]
3.	Norris, F.A., Atkins, R.C. and Majerus, P.W. The cDNA cloning and characterization of inositol polyphosphate 4-phosphatase type II. Evidence for conserved alternative splicing in the 4-phosphatase family. J. Biol. Chem. 272 (1997) 23859–23864. [PMID: 9295334]

[EC 3.1.3.66 created 1992, modified 2002]

3.1.3.67

Accepted name:

phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase

Reaction:

1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H₂O = 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + phosphate

Glossary:

inositol 1,4,5-trisphosphate = Ins(1,4,5)P₃
inositol 1,3,4,5-tetrakisphosphate = Ins(1,3,4,5)P₄
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = PtdIns(4,5)P₂
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate = PtdIns(3,4,5)P₃

Other name(s):

PTEN; MMAC1; phosphatidylinositol-3,4,5-trisphosphate 3-phosphohydrolase

Systematic name:

1-phosphatidyl-1D-myo-inositol-3,4,5-trisphosphate 3-phosphohydrolase

Comments:

Requires Mg²⁺. Does not dephosphorylate inositol 4,5-bisphosphate. This enzyme still works when the 2,3-bis(acyloxy)propyl group is removed, i.e., it hydrolyses Ins(1,3,4,5)P₄ to Ins(1,4,5)P₃

References:

1.	Kabuyama, Y., Nakatsu, N., Homma, Y., Fukui, Y. Purification and characterization of phosphatidyl inositol-3,4,5-trisphosphate phosphatase in bovine thymus. Eur. J. Biochem. 238 (1996) 350–356. [PMID: 8681945]
2.	Maehama, T. and Dixon, J.E. The tumor suppressor, PTEN /MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. J. Biol. Chem. 273 (1998) 13375–13378. [PMID: 9593664]

[EC 3.1.3.67 created 1999, modified 2002]

3.1.3.68

Accepted name:

2-deoxyglucose-6-phosphatase

Reaction:

2-deoxy-D-glucose 6-phosphate + H₂O = 2-deoxy-D-glucose + phosphate

Other name(s):

2-deoxyglucose-6-phosphate phosphatase

Systematic name:

2-deoxy-D-glucose-6-phosphate phosphohydrolase

Comments:

Also active towards fructose 1-phosphate

References:

Johnston, M., Andrews, S., Brinkman, R., Cooper, J., Ding, H., Dover, J., Du, Z., Favello, A., Fulton, L., Gattung, S., Geisel, C., Kirsten, J., Kucaba, T., Hillier, L., Jier, M., Johnston, L., Langston, Y., Latreille, P., Louis, E.J., Macri, C., M , St.Peter, H., Trevaskis, E., Vaughan, K., Vignati, D., Wilcox, L., Wohldman, P., Waterston, R., Wilson, R., Vaudin, M. Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII. Science 265 (1994) 2077–2082. [PMID: 8091229]

Randez-Gil, F., Blasco, A., Prieto, J.A., Sanz, P. DOGR1 and DOGR2: two genes from Saccharomyces cerevisiae that confer 2-deoxyglucose resistance when overexpressed. Yeast 11 (1995) 1233–1240. [PMID: 8553694]

[EC 3.1.3.68 created 1999]

3.1.3.69

Accepted name:

glucosylglycerol 3-phosphatase

Reaction:

2-O-(α-D-glucosyl)-sn-glycerol-3-phosphate + H₂O = 2-O-(α-D-glucopyranosyl)glycerol + phosphate

Other name(s):

salt tolerance protein A; StpA; 2-(β-D-glucosyl)-sn-glycerol-3-phosphate phosphohydrolase (incorrect)

Systematic name:

2-O-(α-D-glucopyranosyl)-sn-glycerol-3-phosphate phosphohydrolase

Comments:

Acts with EC 2.4.1.213 (glucosylglycerol-phosphate synthase) to form glucosylglycerol, an osmolyte that endows cyanobacteria with resistance to salt.

References:

1.	Hagemann, M. and Erdmann, N. Activation and pathway of glucosylglycerol biosynthesis in the cyanobacterium Synechocystis sp. PCC 6803. Microbiology 140 (1994) 1427–1431.
2.	Hagemann, M., Richter, S., Zuther, E. and Schoor, A. Characterization of a glucosylglycerol-phosphate-accumulating salt-sensitive mutant of the cyanobacterium Synechocystis sp. strain PCC 6803. Arch. Microbiol. 166 (1996) 83–91. [PMID: 8772170]
3.	Hagemann, M., Schoor, A., Jeanjean, R., Zuther, E. and Joset, F. The gene stpA from Synechocystis sp. strain PCC 6803 encodes for the glucosylglycerol-phosphate phosphatase involved in cyanobacterial salt adaptation. J. Bacteriol. 179 (1997) 1727–1733. [PMID: 9045835]

[EC 3.1.3.69 created 2001, modified 2015]

3.1.3.70

Accepted name:

mannosyl-3-phosphoglycerate phosphatase

Reaction:

2-O-(α-D-mannosyl)-3-phosphoglycerate + H₂O = 2-O-(α-D-mannosyl)-D-glycerate + phosphate

Systematic name:

2-O-(α-D-mannosyl)-3-phosphoglycerate phosphohydrolase

Comments:

Requires Mg²⁺. The enzyme from Pyrococcus horikoshii is specific for α-D-mannosyl-3-phosphoglycerate and forms part of the pathway for the synthesis of mannosylglycerate.

References:

1.	Empadinhas, N., Marugg, J.D., Borges, N., Santos, H. and da Costa, M.S. Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. Biochemical and genetic characterization of key-enzymes. J. Biol. Chem. 276 (2001) 43580–43588. [PMID: 11562374]

[EC 3.1.3.70 created 2002]

3.1.3.71

Accepted name:

2-phosphosulfolactate phosphatase

Reaction:

(2R)-2-phospho-3-sulfolactate + H₂O = (2R)-3-sulfolactate + phosphate

Other name(s):

(2R)-phosphosulfolactate phosphohydrolase; ComB phosphatase

Systematic name:

(R)-2-phospho-3-sulfolactate phosphohydrolase

Comments:

Requires Mg²⁺. The enzyme from Methanococcus jannaschii acts on both stereoisoimers of the substrate and also hydrolyses a number of phosphate monoesters of (S)-2-hydroxycarboxylic acids, including 2-phosphomalate, 2-phospholactate and 2-phosphoglycolate. This enzyme can also hydrolyse phosphate monoesters of (R)-2-hydroxycarboxylic acids such as (S)-2-phospho-3-sulfolactate and (R)-2-phosphomalate, which, presumably, bind to the enzyme in opposite orientations.

References:

1.	Graham, D.E., Graupner, M., Xu, H. and White, R.H. Identification of coenzyme M biosynthetic 2-phosphosulfolactate phosphatase. Eur. J. Biochem. 268 (2001) 5176–5188. [PMID: 11589710]

[EC 3.1.3.71 created 2002]

3.1.3.72

Accepted name:

5-phytase

Reaction:

myo-inositol hexakisphosphate + H₂O = 1L-myo-inositol 1,2,3,4,6-pentakisphosphate + phosphate

Systematic name:

myo-inositol-hexakisphosphate 5-phosphohydrolase

Comments:

The enzyme attacks the product of the above reaction more slowly to yield Ins(1,2,3)P₃.

References:

1.	Barrientos, L., Scott, J.J. and Murthy, P.P. Specificity of hydrolysis of phytic acid by alkaline phytase from lily pollen. Plant Physiol. 106 (1994) 1489–1495. [PMID: 7846160]

[EC 3.1.3.72 created 2002]

3.1.3.73

Accepted name:

adenosylcobalamin/α-ribazole phosphatase

Reaction:

(1) adenosylcobalamin 5′-phosphate + H₂O = coenzyme B₁₂ + phosphate
(2) α-ribazole 5′-phosphate + H₂O = α-ribazole + phosphate

Other name(s):

CobC; adenosylcobalamin phosphatase; α-ribazole phosphatase

Systematic name:

adenosylcobalamin/α-ribazole-5′-phosphate phosphohydrolase

Comments:

This enzyme catalyses the last step in the anaerobic (early cobalt insertion) pathway of adenosylcobalamin biosynthesis, characterized in Salmonella enterica [3]. It also participates in a salvage pathway that recycles cobinamide into adenosylcobalamin [1].

References:

1.	O'Toole, G.A., Trzebiatowski, J.R. and Escalante-Semerena, J.C. The cobC gene of Salmonella typhimurium codes for a novel phosphatase involved in the assembly of the nucleotide loop of cobalamin. J. Biol. Chem. 269 (1994) 26503–26511. [PMID: 7929373]
2.	Warren, M.J., Raux, E., Schubert, H.L. and Escalante-Semerena, J.C. The biosynthesis of adenosylcobalamin (vitamin B₁₂). Nat. Prod. Rep. 19 (2002) 390–412. [PMID: 12195810]
3.	Zayas, C.L. and Escalante-Semerena, J.C. Reassessment of the late steps of coenzyme B₁₂ synthesis in Salmonella enterica: evidence that dephosphorylation of adenosylcobalamin-5′-phosphate by the CobC phosphatase is the last step of the pathway. J. Bacteriol. 189 (2007) 2210–2218. [PMID: 17209023]

[EC 3.1.3.73 created 2004, modified 2011]

3.1.3.74

Accepted name:

pyridoxal phosphatase

Reaction:

pyridoxal 5′-phosphate + H₂O = pyridoxal + phosphate

Other name(s):

vitamine B₆ (pyridoxine) phosphatase; PLP phosphatase; vitamin B₆-phosphate phosphatase; PNP phosphatase

Systematic name:

pyridoxal-5′-phosphate phosphohydrolase

Comments:

Requires Mg²⁺. This enzyme is specific for phosphorylated vitamin B₆ compounds: it acts not only on pyridoxal phosphate (PLP), but also on pyridoxine phosphate (PNP), pyridoxamine phosphate (PMP), 4-pyridoxic acid phosphate and 4-deoxypyridoxine phosphate. This reaction can also be carried out by EC 3.1.3.1 (alkaline phosphatase) and EC 3.1.3.2 (acid phosphatase), but these enzymes have very broad substrate specificities.

References:

1.	Fonda, M.L. Purification and characterization of vitamin B₆-phosphate phosphatase from human erythrocytes. J. Biol. Chem. 267 (1992) 15978–15983. [PMID: 1322411]
2.	Fonda, M.L. and Zhang, Y.N. Kinetic mechanism and divalent metal activation of human erythrocyte pyridoxal phosphatase. Arch. Biochem. Biophys. 320 (1995) 345–352. [PMID: 7625842]
3.	Jang, Y.M., Kim, D.W., Kang, T.C., Won, M.H., Baek, N.I., Moon, B.J., Choi, S.Y. and Kwon, O.S. Human pyridoxal phosphatase. Molecular cloning, functional expression, and tissue distribution. J. Biol. Chem. 278 (2003) 50040–50046. [PMID: 14522954]

[EC 3.1.3.74 created 2004]

3.1.3.75

Accepted name:

phosphoethanolamine/phosphocholine phosphatase

Reaction:

(1) O-phosphoethanolamine + H₂O = ethanolamine + phosphate
(2) phosphocholine + H₂O = choline + phosphate

Other name(s):

PHOSPHO1; 3X11A

Systematic name:

phosphoethanolamine phosphohydrolase

Comments:

Requires active site Mg²⁺ but also works, to a lesser extent, with Co²⁺ and Mn²⁺. The enzyme is highly specific for phosphoethanolamine and phosphocholine.

References:

1.	Houston, B., Seawright, E., Jefferies, D., Hoogland, E., Lester, D., Whitehead, C. and Farquharson, C. Identification and cloning of a novel phosphatase expressed at high levels in differentiating growth plate chondrocytes. Biochim. Biophys. Acta 1448 (1999) 500–506. [PMID: 9990301]
2.	Stewart, A.J., Schmid, R., Blindauer, C.A., Paisey, S.J. and Farquharson, C. Comparative modelling of human PHOSPHO1 reveals a new group of phosphatases within the haloacid dehalogenase superfamily. Protein Eng. 16 (2003) 889–895. [PMID: 14983068]
3.	Roberts, S.J., Stewart, A.J., Sadler, P.J. and Farquharson, C. Human PHOSPHO1 displays high specific phosphoethanolamine and phosphocholine phosphatase activities. Biochem. J. 382 (2004) 59–65. [PMID: 15175005]

[EC 3.1.3.75 created 2004]

3.1.3.76

Accepted name:

lipid-phosphate phosphatase

Reaction:

(9S,10S)-10-hydroxy-9-(phosphooxy)octadecanoate + H₂O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate

Other name(s):

hydroxy fatty acid phosphatase; dihydroxy fatty acid phosphatase; hydroxy lipid phosphatase; sEH (ambiguous); soluble epoxide hydrolase (ambiguous); (9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate phosphohydrolase

Systematic name:

(9S,10S)-10-hydroxy-9-(phosphooxy)octadecanoate phosphohydrolase

Comments:

Requires Mg²⁺ for maximal activity. The enzyme from mammals is a bifunctional enzyme: the N-terminal domain exhibits lipid-phosphate-phosphatase activity and the C-terminal domain has the activity of EC 3.3.2.10, soluble epoxide hydrolase (sEH) [1]. The best substrates for this enzyme are 10-hydroxy-9-(phosphooxy)octadecanoates, with the threo- form being a better substrate than the erythro- form [1]. The phosphatase activity is not found in plant sEH or in EC 3.3.2.9, microsomal epoxide hydrolase, from mammals [1].

References:

1.	Newman, J.W., Morisseau, C., Harris, T.R. and Hammock, B.D. The soluble epoxide hydrolase encoded by EPXH₂ is a bifunctional enzyme with novel lipid phosphate phosphatase activity. Proc. Natl. Acad. Sci. USA 100 (2003) 1558–1563. [PMID: 12574510]
2.	Cronin, A., Mowbray, S., Dürk, H., Homburg, S., Fleming, I., Fisslthaler, B., Oesch, F. and Arand, M. The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase. Proc. Natl. Acad. Sci. USA 100 (2003) 1552–1557. [PMID: 12574508]
3.	Morisseau, C. and Hammock, B.D. Epoxide hydrolases: mechanisms, inhibitor designs, and biological roles. Annu. Rev. Pharmacol. Toxicol. 45 (2005) 311–333. [PMID: 15822179]
4.	Tran, K.L., Aronov, P.A., Tanaka, H., Newman, J.W., Hammock, B.D. and Morisseau, C. Lipid sulfates and sulfonates are allosteric competitive inhibitors of the N-terminal phosphatase activity of the mammalian soluble epoxide hydrolase. Biochemistry 44 (2005) 12179–12187. [PMID: 16142916]
5.	Newman, J.W., Morisseau, C. and Hammock, B.D. Epoxide hydrolases: their roles and interactions with lipid metabolism. Prog. Lipid Res. 44 (2005) 1–51. [PMID: 15748653]
6.	Srivastava, P.K., Sharma, V.K., Kalonia, D.S. and Grant, D.F. Polymorphisms in human soluble epoxide hydrolase: effects on enzyme activity, enzyme stability, and quaternary structure. Arch. Biochem. Biophys. 427 (2004) 164–169. [PMID: 15196990]
7.	Gomez, G.A., Morisseau, C., Hammock, B.D. and Christianson, D.W. Structure of human epoxide hydrolase reveals mechanistic inferences on bifunctional catalysis in epoxide and phosphate ester hydrolysis. Biochemistry 43 (2004) 4716–4723. [PMID: 15096040]

[EC 3.1.3.76 created 2006]

3.1.3.77

Accepted name:

acireductone synthase

Reaction:

5-(methylsulfanyl)-2,3-dioxopentyl phosphate + H₂O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate (overall reaction)
(1a) 5-(methylsulfanyl)-2,3-dioxopentyl phosphate = 2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl phosphate (probably spontaneous)
(1b) 2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl phosphate + H₂O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate

Glossary:

acireductone = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one

Other name(s):

E1; E-1 enolase-phosphatase; 5-(methylthio)-2,3-dioxopentyl-phosphate phosphohydrolase (isomerizing)

Systematic name:

5-(methylsulfanyl)-2,3-dioxopentyl-phosphate phosphohydrolase (isomerizing)

Comments:

This bifunctional enzyme first enolizes the substrate to form the intermediate 2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl phosphate, which is then dephosphorylated to form the acireductone 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one [2]. The acireductone represents a branch point in the methione-salvage pathway as it is used in the formation of formate, CO and 3-(methylsulfanyl)propanoate by EC 1.13.11.53 [acireductone dioxygenase (Ni²⁺-requiring)] and of formate and 4-(methylsulfanyl)-2-oxobutanoate either by a spontaneous reaction under aerobic conditions or by EC 1.13.11.54 {acireductone dioxygenase [iron(II)-requiring]} [1,2].

References:

1.	Myers, R.W., Wray, J.W., Fish, S. and Abeles, R.H. Purification and characterization of an enzyme involved in oxidative carbon-carbon bond cleavage reactions in the methionine salvage pathway of Klebsiella pneumoniae. J. Biol. Chem. 268 (1993) 24785–24791. [PMID: 8227039]
2.	Wray, J.W. and Abeles, R.H. The methionine salvage pathway in Klebsiella pneumoniae and rat liver. Identification and characterization of two novel dioxygenases. J. Biol. Chem. 270 (1995) 3147–3153. [PMID: 7852397]
3.	Wang, H., Pang, H., Bartlam, M. and Rao, Z. Crystal structure of human E1 enzyme and its complex with a substrate analog reveals the mechanism of its phosphatase/enolase activity. J. Mol. Biol. 348 (2005) 917–926. [PMID: 15843022]

[EC 3.1.3.77 created 2006]

3.1.3.78

Accepted name:

phosphatidylinositol-4,5-bisphosphate 4-phosphatase

Reaction:

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H₂O = 1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate

Glossary:

1-phosphatidyl-1D-myo-inositol 3-phosphate = PtdIns3P
1-phosphatidyl-1D-myo-inositol 4-phosphate = PtdIns4P
1-phosphatidyl-1D-myo-inositol 5-phosphate = PtdIns5P
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate = PtdIns(3,4)P₂
1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate = PtdIns(3,5)P₂
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = PtdIns(4,5)P₂
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate = PtdIns(3,4,5)P₃

Other name(s):

phosphatidylinositol-4,5-bisphosphate 4-phosphatase I; phosphatidylinositol-4,5-bisphosphate 4-phosphatase II; type I PtdIns-4,5-P₂ 4-Ptase; type II PtdIns-4,5-P₂ 4-Ptase; IpgD; PtdIns-4,5-P₂ 4-phosphatase type I; PtdIns-4,5-P₂ 4-phosphatase type II; type I phosphatidylinositol-4,5-bisphosphate 4-phosphatase; type 1 4-phosphatase

Systematic name:

1-phosphatidyl-1D-myo-inositol-4,5-bisphosphate 4-phosphohydrolase

Comments:

Two pathways exist in mammalian cells to degrade 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate [PtdIns(4,5)P₂] [2]. One is catalysed by this enzyme and the other by EC 3.1.3.36, phosphoinositide 5-phosphatase, where the product is PtdIns4P. The enzyme from human is specific for PtdIns(4,5)P₂ as substrate, as it cannot use PtdIns(3,4,5)P₃, PtdIns(3,4)P₂, PtdIns(3,5)P₂, PtdIns5P, PtdIns4P or PtdIns3P [2]. In humans, the enzyme is localized to late endosomal/lysosomal membranes [2]. It can control nuclear levels of PtdIns5P and thereby control p53-dependent apoptosis [3].

References:

1.	Niebuhr, K., Giuriato, S., Pedron, T., Philpott, D.J., Gaits, F., Sable, J., Sheetz, M.P., Parsot, C., Sansonetti, P.J. and Payrastre, B. Conversion of PtdIns(4,5)P₂ into PtdIns(5)P by the S. flexneri effector IpgD reorganizes host cell morphology. EMBO J. 21 (2002) 5069–5078. [PMID: 12356723]
2.	Ungewickell, A., Hugge, C., Kisseleva, M., Chang, S.C., Zou, J., Feng, Y., Galyov, E.E., Wilson, M. and Majerus, P.W. The identification and characterization of two phosphatidylinositol-4,5-bisphosphate 4-phosphatases. Proc. Natl. Acad. Sci. USA 102 (2005) 18854–18859. [PMID: 16365287]
3.	Zou, J., Marjanovic, J., Kisseleva, M.V., Wilson, M. and Majerus, P.W. Type I phosphatidylinositol-4,5-bisphosphate 4-phosphatase regulates stress-induced apoptosis. Proc. Natl. Acad. Sci. USA 104 (2007) 16834–16839. [PMID: 17940011]
4.	Mason, D., Mallo, G.V., Terebiznik, M.R., Payrastre, B., Finlay, B.B., Brumell, J.H., Rameh, L. and Grinstein, S. Alteration of epithelial structure and function associated with PtdIns(4,5)P₂ degradation by a bacterial phosphatase. J. Gen. Physiol. 129 (2007) 267–283. [PMID: 17389247]

[EC 3.1.3.78 created 2008]

3.1.3.79

Accepted name:

mannosylfructose-phosphate phosphatase

Reaction:

β-D-fructofuranosyl-α-D-mannopyranoside 6^F-phosphate + H₂O = β-D-fructofuranosyl-α-D-mannopyranoside + phosphate

Glossary:

mannosylfructose = β-D-fructofuranosyl-α-D-mannopyranoside

Other name(s):

mannosylfructose-6-phosphate phosphatase; MFPP

Systematic name:

β-D-fructofuranosyl-α-D-mannopyranoside-6F-phosphate phosphohydrolase

Comments:

This enzyme, from the soil proteobacterium and plant pathogen Agrobacterium tumefaciens strain C58, requires Mg²⁺ for activity. Mannosylfructose is the major endogenous osmolyte produced by several α-proteobacteria in response to osmotic stress and is synthesized by the sequential action of EC 2.4.1.246 (mannosylfructose-phosphate synthase) followed by this enzyme. While mannosylfructose 6-phosphate is the physiological substrate, the enzyme can use sucrose 6-phosphate very efficiently. The F in mannosylfructose 6^F-phosphate is used to indicate that the fructose residue of sucrose carries the substituent.

References:

1.	Torres, L.L. and Salerno, G.L. A metabolic pathway leading to mannosylfructose biosynthesis in Agrobacterium tumefaciens uncovers a family of mannosyltransferases. Proc. Natl. Acad. Sci. USA 104 (2007) 14318–14323. [PMID: 17728402]

[EC 3.1.3.79 created 2009]

3.1.3.80

Accepted name:

2,3-bisphosphoglycerate 3-phosphatase

Reaction:

2,3-bisphospho-D-glycerate + H₂O = 2-phospho-D-glycerate + phosphate

Other name(s):

MIPP1; 2,3-BPG 3-phosphatase

Systematic name:

2,3-bisphospho-D-glycerate 3-phosphohydrolase

Comments:

This reaction is a shortcut in the Rapoport-Luebering shunt. It bypasses the reactions of EC 5.4.2.11/EC 5.4.2.12 [phosphoglycerate mutases (2,3-diphosphoglycerate-dependent and independent)] and directly forms 2-phospho-D-glycerate by removing the 3-phospho-group of 2,3-diphospho-D-glycerate [1]. The MIPP1 protein also catalyses the reaction of EC 3.1.3.62 (multiple inositol-polyphosphate phosphatase).

References:

1.	Cho, J., King, J.S., Qian, X., Harwood, A.J. and Shears, S.B. Dephosphorylation of 2,3-bisphosphoglycerate by MIPP expands the regulatory capacity of the Rapoport-Luebering glycolytic shunt. Proc. Natl. Acad. Sci. USA 105 (2008) 5998–6003. [PMID: 18413611]

[EC 3.1.3.80 created 2010]

3.1.3.81

Accepted name:

diacylglycerol diphosphate phosphatase

Reaction:

1,2-diacyl-sn-glycerol 3-diphosphate + H₂O = 1,2-diacyl-sn-glycerol 3-phosphate + phosphate

Other name(s):

DGPP phosphatase; DGPP phosphohydrolase; DPP1; DPPL1; DPPL2; PAP2; pyrophosphate phosphatase

Systematic name:

1,2-diacyl-sn-glycerol 3-phosphate phosphohydrolase

Comments:

The bifunctional enzyme catalyses the dephosphorylation of diacylglycerol diphosphate to phosphatidate and the subsequent dephosphorylation of phosphatidate to diacylglycerol (cf. phosphatidate phosphatase (EC 3.1.3.4)). It regulates intracellular levels of diacylglycerol diphosphate and phosphatidate, phospholipid molecules believed to play a signalling role in stress response [6]. The phosphatase activity of the bifunctional enzyme is Mg²⁺-independent and N-ethylmaleimide-insensitive and is distinct from the Mg²⁺-dependent and N-ethylmaleimide-sensitive enzyme EC 3.1.3.4 (phosphatidate phosphatase) [5].The diacylglycerol pyrophosphate phosphatase activity in Saccharomyces cerevisiae is induced by zinc depletion, by inositol supplementation, and when cells enter the stationary phase [4].

References:

1.	Dillon, D.A., Wu, W.I., Riedel, B., Wissing, J.B., Dowhan, W. and Carman, G.M. The Escherichia coli pgpB gene encodes for a diacylglycerol pyrophosphate phosphatase activity. J. Biol. Chem. 271 (1996) 30548–30553. [PMID: 8940025]
2.	Dillon, D.A., Chen, X., Zeimetz, G.M., Wu, W.I., Waggoner, D.W., Dewald, J., Brindley, D.N. and Carman, G.M. Mammalian Mg²⁺-independent phosphatidate phosphatase (PAP2) displays diacylglycerol pyrophosphate phosphatase activity. J. Biol. Chem. 272 (1997) 10361–10366. [PMID: 9099673]
3.	Wu, W.I., Liu, Y., Riedel, B., Wissing, J.B., Fischl, A.S. and Carman, G.M. Purification and characterization of diacylglycerol pyrophosphate phosphatase from Saccharomyces cerevisiae. J. Biol. Chem. 271 (1996) 1868–1876. [PMID: 8567632]
4.	Oshiro, J., Han, G.S. and Carman, G.M. Diacylglycerol pyrophosphate phosphatase in Saccharomyces cerevisiae. Biochim. Biophys. Acta 1635 (2003) 1–9. [PMID: 14642771]
5.	Carman, G.M. Phosphatidate phosphatases and diacylglycerol pyrophosphate phosphatases in Saccharomyces cerevisiae and Escherichia coli. Biochim. Biophys. Acta 1348 (1997) 45–55. [PMID: 9370315]
6.	Han, G.S., Johnston, C.N., Chen, X., Athenstaedt, K., Daum, G. and Carman, G.M. Regulation of the Saccharomyces cerevisiae DPP1-encoded diacylglycerol pyrophosphate phosphatase by zinc. J. Biol. Chem. 276 (2001) 10126–10133. [PMID: 11139591]

[EC 3.1.3.81 created 2010]

3.1.3.82

Accepted name:

D-glycero-β-D-manno-heptose 1,7-bisphosphate 7-phosphatase

Reaction:

D-glycero-β-D-manno-heptose 1,7-bisphosphate + H₂O = D-glycero-β-D-manno-heptose 1-phosphate + phosphate

Other name(s):

gmhB (gene name); yaeD (gene name)

Systematic name:

D-glycero-β-D-manno-heptose 1,7-bisphosphate 7-phosphohydrolase

Comments:

The enzyme is involved in biosynthesis of ADP-L-glycero-β-D-manno-heptose, which is utilized for assembly of the lipopolysaccharide inner core in Gram-negative bacteria. In vitro the catalytic efficiency with the β-anomer is 100-200-fold higher than with the α-anomer [3].

References:

1.	Kneidinger, B., Marolda, C., Graninger, M., Zamyatina, A., McArthur, F., Kosma, P., Valvano, M.A. and Messner, P. Biosynthesis pathway of ADP-L-glycero-β-D-manno-heptose in Escherichia coli. J. Bacteriol. 184 (2002) 363–369. [PMID: 11751812]
2.	Valvano, M.A., Messner, P. and Kosma, P. Novel pathways for biosynthesis of nucleotide-activated glycero-manno-heptose precursors of bacterial glycoproteins and cell surface polysaccharides. Microbiology 148 (2002) 1979–1989. [PMID: 12101286]
3.	Wang, L., Huang, H., Nguyen, H.H., Allen, K.N., Mariano, P.S. and Dunaway-Mariano, D. Divergence of biochemical function in the HAD superfamily: D-glycero-D-manno-heptose-1,7-bisphosphate phosphatase (GmhB). Biochemistry 49 (2010) 1072–1081. [PMID: 20050615]

[EC 3.1.3.82 created 2010]

3.1.3.83

Accepted name:

D-glycero-α-D-manno-heptose 1,7-bisphosphate 7-phosphatase

Reaction:

D-glycero-α-D-manno-heptose 1,7-bisphosphate + H₂O = D-glycero-α-D-manno-heptose 1-phosphate + phosphate

Other name(s):

gmhB (gene name)

Systematic name:

D-glycero-α-D-manno-heptose 1,7-bisphosphate 7-phosphohydrolase

Comments:

The enzyme is involved in biosynthesis of GDP-D-glycero-α-D-manno-heptose, which is required for assembly of S-layer glycoprotein in some Gram-positive bacteria. The in vitro catalytic efficiency of the enzyme from Bacteroides thetaiotaomicron is 6-fold higher with the α-anomer than with the β-anomer [1].

References:

1.	Wang, L., Huang, H., Nguyen, H.H., Allen, K.N., Mariano, P.S. and Dunaway-Mariano, D. Divergence of biochemical function in the HAD superfamily: D-glycero-D-manno-heptose-1,7-bisphosphate phosphatase (GmhB). Biochemistry 49 (2010) 1072–1081. [PMID: 20050615]

[EC 3.1.3.83 created 2010]

3.1.3.84

Accepted name:

ADP-ribose 1′′-phosphate phosphatase

Reaction:

ADP-D-ribose 1′′-phosphate + H₂O = ADP-D-ribose + phosphate

Other name(s):

POA1; Appr1p phosphatase; Poa1p; ADP-ribose 1′′-phosphate phosphohydrolase

Systematic name:

ADP-D-ribose 1′′-phosphate phosphohydrolase

Comments:

The enzyme is highly specific for ADP-D-ribose 1′′-phosphate. Involved together with EC 3.1.4.37, 2′,3′-cyclic-nucleotide 3′-phosphodiesterase, in the breakdown of adenosine diphosphate ribose 1′′,2′′-cyclic phosphate (Appr>p), a by-product of tRNA splicing.

References:

1.	Shull, N.P., Spinelli, S.L. and Phizicky, E.M. A highly specific phosphatase that acts on ADP-ribose 1′′-phosphate, a metabolite of tRNA splicing in Saccharomyces cerevisiae. Nucleic Acids Res. 33 (2005) 650–660. [PMID: 15684411]

[EC 3.1.3.84 created 2011]

3.1.3.85

Accepted name:

glucosyl-3-phosphoglycerate phosphatase

Reaction:

2-O-(α-D-glucopyranosyl)-3-phospho-D-glycerate + H₂O = 2-O-(α-D-glucopyranosyl)-D-glycerate + phosphate

Other name(s):

GpgP protein

Systematic name:

α-D-glucosyl-3-phospho-D-glycerate phosphohydrolase

Comments:

The enzyme is involved in biosynthesis of 2-O-(α-D-glucopyranosyl)-D-glycerate via the two-step pathway in which EC 2.4.1.266 (glucosyl-3-phosphoglycerate synthase) catalyses the conversion of GDP-glucose and 3-phospho-D-glycerate into 2-O-(α-D-glucopyranosyl)-3-phospho-D-glycerate, which is then converted to 2-O-(α-D-glucopyranosyl)-D-glycerate by glucosyl-3-phosphoglycerate phosphatase. In vivo the enzyme catalyses the dephosphorylation of 2-O-(α-D-mannopyranosyl)-3-phospho-D-glycerate with lower efficiency [1,2]. Divalent metal ions (Mg²⁺, Mn²⁺ or Co²⁺) stimulate activity [1,2].

References:

1.	Costa, J., Empadinhas, N. and da Costa, M.S. Glucosylglycerate biosynthesis in the deepest lineage of the bacteria: characterization of the thermophilic proteins GpgS and GpgP from Persephonella marina. J. Bacteriol. 189 (2007) 1648–1654. [PMID: 17189358]
2.	Costa, J., Empadinhas, N., Goncalves, L., Lamosa, P., Santos, H. and da Costa, M.S. Characterization of the biosynthetic pathway of glucosylglycerate in the archaeon Methanococcoides burtonii. J. Bacteriol. 188 (2006) 1022–1030. [PMID: 16428406]
3.	Mendes, V., Maranha, A., Alarico, S., da Costa, M.S. and Empadinhas, N. Mycobacterium tuberculosis Rv2419c, the missing glucosyl-3-phosphoglycerate phosphatase for the second step in methylglucose lipopolysaccharide biosynthesis. Sci. Rep. 1:177 (2011). [PMID: 22355692]

[EC 3.1.3.85 created 2011]

3.1.3.86

Accepted name:

phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase

Reaction:

1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H₂O = 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate

Glossary:

1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate = PtdIns(3,4)P₂
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate = PtdIns(3,4,5)P₃
1-phosphatidyl-1D-myo-inositol 1,3,4,5-trisphosphate = PtdIns(1,3,4,5)P₄

Other name(s):

SHIP1; SHIP2; SHIP; p150Ship

Systematic name:

1-phosphatidyl-1D-myo-inositol-3,4,5-trisphosphate 5-phosphohydrolase

Comments:

This enzyme hydrolyses 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate (PtdIns(3,4,5)P₃) to produce PtdIns(3,4)P₂, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. The enzyme also shows activity toward (PtdIns(1,3,4,5)P₄) [5]. The enzyme is involved in several signal transduction pathways in the immune system leading to an adverse range of effects.

References:

1.	Lioubin, M.N., Algate, P.A., Tsai, S., Carlberg, K., Aebersold, A. and Rohrschneider, L.R. p150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity. Genes Dev. 10 (1996) 1084–1095. [PMID: 8654924]
2.	Damen, J.E., Liu, L., Rosten, P., Humphries, R.K., Jefferson, A.B., Majerus, P.W. and Krystal, G. The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-triphosphate 5-phosphatase. Proc. Natl. Acad. Sci. USA 93 (1996) 1689–1693. [PMID: 8643691]
3.	Giuriato, S., Payrastre, B., Drayer, A.L., Plantavid, M., Woscholski, R., Parker, P., Erneux, C. and Chap, H. Tyrosine phosphorylation and relocation of SHIP are integrin-mediated in thrombin-stimulated human blood platelets. J. Biol. Chem. 272 (1997) 26857–26863. [PMID: 9341117]
4.	Drayer, A.L., Pesesse, X., De Smedt, F., Woscholski, R., Parker, P. and Erneux, C. Cloning and expression of a human placenta inositol 1,3,4,5-tetrakisphosphate and phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase. Biochem. Biophys. Res. Commun. 225 (1996) 243–249. [PMID: 8769125]
5.	Pesesse, X., Moreau, C., Drayer, A.L., Woscholski, R., Parker, P. and Erneux, C. The SH₂ domain containing inositol 5-phosphatase SHIP2 displays phosphatidylinositol 3,4,5-trisphosphate and inositol 1,3,4,5-tetrakisphosphate 5-phosphatase activity. FEBS Lett. 437 (1998) 301–303. [PMID: 9824312]

[EC 3.1.3.86 created 2011]

3.1.3.87

Accepted name:

2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase

Reaction:

2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-en-1-yl phosphate + H₂O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate

Other name(s):

HK-MTPenyl-1-P phosphatase; MtnX; YkrX; 2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate phosphohydrolase; 2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl phosphate phosphohydrolase

Systematic name:

2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-en-1-yl phosphate phosphohydrolase

Comments:

The enzyme participates in the methionine salvage pathway in Bacillus subtilis [2]. In some species a single bifunctional enzyme, EC 3.1.3.77, acireductone synthase, catalyses both this reaction and EC 5.3.2.5, 2,3-diketo-5-methylthiopentyl-1-phosphate enolase [1].

References:

1.	Myers, R.W., Wray, J.W., Fish, S. and Abeles, R.H. Purification and characterization of an enzyme involved in oxidative carbon-carbon bond cleavage reactions in the methionine salvage pathway of Klebsiella pneumoniae. J. Biol. Chem. 268 (1993) 24785–24791. [PMID: 8227039]
2.	Ashida, H., Saito, Y., Kojima, C., Kobayashi, K., Ogasawara, N. and Yokota, A. A functional link between RuBisCO-like protein of Bacillus and photosynthetic RuBisCO. Science 302 (2003) 286–290. [PMID: 14551435]

[EC 3.1.3.87 created 2012]

3.1.3.88

Accepted name:

5′′-phosphoribostamycin phosphatase

Reaction:

5′′-phosphoribostamycin + H₂O = ribostamycin + phosphate

Other name(s):

btrP (gene name); neoI (gene name)

Systematic name:

5′′-phosphoribostamycin phosphohydrolase

Comments:

Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including ribostamycin, neomycin and butirosin. No metal is required for activity.

References:

1.	Kudo, F., Fujii, T., Kinoshita, S. and Eguchi, T. Unique O-ribosylation in the biosynthesis of butirosin. Bioorg. Med. Chem. 15 (2007) 4360–4368. [PMID: 17482823]

[EC 3.1.3.88 created 2012]

3.1.3.89

Accepted name:

5′-deoxynucleotidase

Reaction:

a 2′-deoxyribonucleoside 5′-monophosphate + H₂O = a 2′-deoxyribonucleoside + phosphate

Other name(s):

yfbR (gene name)

Systematic name:

2′-deoxyribonucleoside 5′-monophosphate phosphohydrolase

Comments:

The enzyme, characterized from the bacterium Escherichia coli, shows strict specificity towards deoxyribonucleoside 5′-monophosphates and does not dephosphorylate 5′-ribonucleotides or ribonucleoside 3′-monophosphates. A divalent metal cation is required for activity, with cobalt providing the highest activity.

References:

1.	Proudfoot, M., Kuznetsova, E., Brown, G., Rao, N.N., Kitagawa, M., Mori, H., Savchenko, A. and Yakunin, A.F. General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG. J. Biol. Chem. 279 (2004) 54687–54694. [PMID: 15489502]
2.	Zimmerman, M.D., Proudfoot, M., Yakunin, A. and Minor, W. Structural insight into the mechanism of substrate specificity and catalytic activity of an HD-domain phosphohydrolase: the 5′-deoxyribonucleotidase YfbR from Escherichia coli. J. Mol. Biol. 378 (2008) 215–226. [PMID: 18353368]

[EC 3.1.3.89 created 2013]

3.1.3.90

Accepted name:

maltose 6′-phosphate phosphatase

Reaction:

maltose 6′-phosphate + H₂O = maltose + phosphate

Other name(s):

maltose 6′-P phosphatase; mapP (gene name)

Systematic name:

maltose 6′-phosphate phosphohydrolase

Comments:

The enzyme from the bacterium Enterococcus faecalis also has activity with the sucrose isomer turanose 6′-phosphate (α-D-glucopyranosyl-(1→3)-D-fructose 6-phosphate).

References:

Mokhtari, A., Blancato, V.S., Repizo, G.D., Henry, C., Pikis, A., Bourand, A., de Fatima Alvarez, M., Immel, S., Mechakra-Maza, A., Hartke, A., Thompson, J., Magni, C. and Deutscher, J. Enterococcus faecalis utilizes maltose by connecting two incompatible metabolic routes via a novel maltose 6′-phosphate phosphatase (MapP). Mol. Microbiol. 88 (2013) 234–253. [PMID: 23490043]

[EC 3.1.3.90 created 2013]

3.1.3.91

Accepted name:

7-methylguanosine nucleotidase

Reaction:

(1) N⁷-methyl-GMP + H₂O = N⁷-methyl-guanosine + phosphate
(2) CMP + H₂O = cytidine + phosphate

Other name(s):

cytosolic nucleotidase III-like; cNIII-like; N⁷-methylguanylate 5′-phosphatase

Systematic name:

N⁷-methyl-GMP phosphohydrolase

Comments:

The enzyme also has low activity with N⁷-methyl-GDP, producing N⁷-methyl-GMP. Does not accept AMP or GMP, and has low activity with UMP.

References:

1.	Buschmann, J., Moritz, B., Jeske, M., Lilie, H., Schierhorn, A. and Wahle, E. Identification of Drosophila and human 7-methyl GMP-specific nucleotidases. J. Biol. Chem. 288 (2013) 2441–2451. [PMID: 23223233]

[EC 3.1.3.91 created 2013]

3.1.3.92

Accepted name:

kanosamine-6-phosphate phosphatase

Reaction:

kanosamine 6-phosphate + H₂O = kanosamine + phosphate

Glossary:

kanosamine = 3-amino-3-deoxy-D-glucose

Other name(s):

ntdB (gene name)

Systematic name:

kanosamine-6-phosphate phosphohydrolase

Comments:

The enzyme, found in the bacterium Bacillus subtilis, is involved in a kanosamine biosynthesis pathway.

References:

Vetter, N.D., Langill, D.M., Anjum, S., Boisvert-Martel, J., Jagdhane, R.C., Omene, E., Zheng, H., van Straaten, K.E., Asiamah, I., Krol, E.S., Sanders, D.A. and Palmer, D.R. A previously unrecognized kanosamine biosynthesis pathway in Bacillus subtilis. J. Am. Chem. Soc. 135 (2013) 5970–5973. [PMID: 23586652]

[EC 3.1.3.92 created 2013]

3.1.3.93

Accepted name:

L-galactose 1-phosphate phosphatase

Reaction:

β-L-galactose 1-phosphate + H₂O = L-galactose + phosphate

Other name(s):

VTC4 (gene name) (ambiguous); IMPL2 (gene name) (ambiguous)

Systematic name:

β-L-galactose-1-phosphate phosphohydrolase

Comments:

The enzyme from plants also has the activity of EC 3.1.3.25, inositol-phosphate phosphatase. The enzymes have very low activity with D-galactose 1-phosphate (cf. EC 3.1.3.94, D-galactose 1-phosphate phosphatase).

References:

1.	Laing, W.A., Bulley, S., Wright, M., Cooney, J., Jensen, D., Barraclough, D. and MacRae, E. A highly specific L-galactose-1-phosphate phosphatase on the path to ascorbate biosynthesis. Proc. Natl. Acad. Sci. USA 101 (2004) 16976–16981. [PMID: 15550539]
2.	Torabinejad, J., Donahue, J.L., Gunesekera, B.N., Allen-Daniels, M.J. and Gillaspy, G.E. VTC4 is a bifunctional enzyme that affects myoinositol and ascorbate biosynthesis in plants. Plant Physiol. 150 (2009) 951–961. [PMID: 19339506]
3.	Petersen, L.N., Marineo, S., Mandala, S., Davids, F., Sewell, B.T. and Ingle, R.A. The missing link in plant histidine biosynthesis: Arabidopsis myoinositol monophosphatase-like2 encodes a functional histidinol-phosphate phosphatase. Plant Physiol. 152 (2010) 1186–1196. [PMID: 20023146]

[EC 3.1.3.93 created 2014]

3.1.3.94

Accepted name:

D-galactose 1-phosphate phosphatase

Reaction:

α-D-galactose 1-phosphate + H₂O = D-galactose + phosphate

Systematic name:

α-D-galactose-1-phosphate phosphohydrolase

Comments:

The human enzyme also has the activity of EC 3.1.3.25, inositol-phosphate phosphatase. The enzyme has very low activity with L-galactose 1-phosphate (cf. EC 3.1.3.93, L-galactose 1-phosphate phosphatase).

References:

1.	Parthasarathy, R., Parthasarathy, L. and Vadnal, R. Brain inositol monophosphatase identified as a galactose 1-phosphatase. Brain Res. 778 (1997) 99–106. [PMID: 9462881]

[EC 3.1.3.94 created 2014]

3.1.3.95

Accepted name:

phosphatidylinositol-3,5-bisphosphate 3-phosphatase

Reaction:

1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H₂O = 1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate

Glossary:

1-phosphatidyl-1D-myo-inositol 5-phosphate = PtdIns5P
1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate = PtdIns(3,5)P₂

Other name(s):

MTMR; PtdIns-3,5-P₂ 3-Ptase

Systematic name:

1-phosphatidyl-1D-myo-inositol-3,5-bisphosphate 3-phosphohydrolase

Comments:

The enzyme is found in both plants and animals. It also has the activity of EC 3.1.3.64 (phosphatidylinositol-3-phosphatase).

References:

1.	Walker, D.M., Urbe, S., Dove, S.K., Tenza, D., Raposo, G. and Clague, M.J. Characterization of MTMR3. an inositol lipid 3-phosphatase with novel substrate specificity. Curr. Biol. 11 (2001) 1600–1605. [PMID: 11676921]
2.	Berger, P., Bonneick, S., Willi, S., Wymann, M. and Suter, U. Loss of phosphatase activity in myotubularin-related protein 2 is associated with Charcot-Marie-Tooth disease type 4B1. Hum. Mol. Genet. 11 (2002) 1569–1579. [PMID: 12045210]
3.	Ding, Y., Lapko, H., Ndamukong, I., Xia, Y., Al-Abdallat, A., Lalithambika, S., Sadder, M., Saleh, A., Fromm, M., Riethoven, J.J., Lu, G. and Avramova, Z. The Arabidopsis chromatin modifier ATX1, the myotubularin-like AtMTM and the response to drought. Plant Signal. Behav. 4 (2009) 1049–1058. [PMID: 19901554]

[EC 3.1.3.95 created 2014]

3.1.3.96

Accepted name:

pseudouridine 5′-phosphatase

Reaction:

pseudouridine 5′-phosphate + H₂O = pseudouridine + phosphate

Other name(s):

pseudouridine 5′-monophosphatase; 5′-PsiMPase; HDHD1

Systematic name:

pseudouridine 5′-phosphohydrolase

Comments:

Requires Mg²⁺ for activity.

References:

1.	Preumont, A., Rzem, R., Vertommen, D. and Van Schaftingen, E. HDHD1, which is often deleted in X-linked ichthyosis, encodes a pseudouridine-5′-phosphatase. Biochem. J. 431 (2010) 237–244. [PMID: 20722631]

[EC 3.1.3.96 created 2014]

3.1.3.97

Accepted name:

3′,5′-nucleoside bisphosphate phosphatase

Reaction:

nucleoside 3′,5′-bisphosphate + H₂O = nucleoside 5′-phosphate + phosphate

Systematic name:

nucleoside-3′,5′-bisphosphate 3′-phosphohydrolase

Comments:

The enzyme, characterized from the bacterium Chromobacterium violaceum, has similar catalytic efficiencies with all the bases. The enzyme has similar activity with ribonucleoside and 2′-deoxyribonucleoside 3′,5′-bisphosphates, but shows no activity with nucleoside 2′,5′-bisphosphates (cf. EC 3.1.3.7, 3′(2′),5′-bisphosphate nucleotidase).

References:

1.	Cummings, J.A., Vetting, M., Ghodge, S.V., Xu, C., Hillerich, B., Seidel, R.D., Almo, S.C. and Raushel, F.M. Prospecting for unannotated enzymes: discovery of a 3′,5′-nucleotide bisphosphate phosphatase within the amidohydrolase superfamily. Biochemistry 53 (2014) 591–600. [PMID: 24401123]

[EC 3.1.3.97 created 2015]

3.1.3.98

Transferred entry:

geranyl diphosphate phosphohydrolase, transferred to EC 3.6.1.68, geranyl diphosphate phosphohydrolase

[EC 3.1.3.98 created 2015, deleted 2016]

3.1.3.99

Accepted name:

IMP-specific 5′-nucleotidase

Reaction:

IMP + H₂O = inosine + phosphate

Other name(s):

ISN1 (gene name)

Systematic name:

inosine 5′-phosphate phosphohydrolase

Comments:

The enzyme, isolated from the yeast Saccharomyces cerevisiae, is highly specific for inosine 5′-phosphate, and has no detectable activity with other purine and pyrimidine nucleotides. Requires divalent metals, such as Mg²⁺, Co²⁺ or Mn²⁺.

References:

1.	Itoh, R. Purification and some properties of an IMP-specific 5′-nucleotidase from yeast. Biochem. J. 298 (1994) 593–598. [PMID: 8141771]
2.	Itoh, R., Saint-Marc, C., Chaignepain, S., Katahira, R., Schmitter, J.M. and Daignan-Fornier, B. The yeast ISN1 (YOR155c) gene encodes a new type of IMP-specific 5′-nucleotidase. BMC Biochem. 4:4 (2003). [PMID: 12735798]

[EC 3.1.3.99 created 2016]

3.1.3.100

Accepted name:

thiamine phosphate phosphatase

Reaction:

thiamine phosphate + H₂O = thiamine + phosphate

Systematic name:

thiamine phosphate phosphohydrolase

Comments:

The enzyme participates in the thiamine biosynthesis pathway in eukaryotes and a few prokaryotes. These organisms lack EC 2.7.4.16, thiamine-phosphate kinase, and need to convert thiamine phosphate to thiamine diphosphate, the active form of the vitamin, by first removing the phosphate group, followed by diphosphorylation by EC 2.7.6.2, thiamine diphosphokinase.

References:

1.	Sanemori, H., Egi, Y. and Kawasaki, T. Pathway of thiamine pyrophosphate synthesis in Micrococcus denitrificans. J. Bacteriol. 126 (1976) 1030–1036. [PMID: 181359]
2.	Komeda, Y., Tanaka, M. and Nishimune, T. A th-1 mutant of Arabidopsis thaliana is defective for a thiamin-phosphate-synthesizing enzyme: thiamin phosphate pyrophosphorylase. Plant Physiol. 88 (1988) 248–250. [PMID: 16666289]
3.	Schweingruber, A.M., Dlugonski, J., Edenharter, E. and Schweingruber, M.E. Thiamine in Schizosaccharomyces pombe: dephosphorylation, intracellular pool, biosynthesis and transport. Curr. Genet. 19 (1991) 249–254. [PMID: 1868574]
4.	Muller, I.B., Bergmann, B., Groves, M.R., Couto, I., Amaral, L., Begley, T.P., Walter, R.D. and Wrenger, C. The vitamin B₁ metabolism of Staphylococcus aureus is controlled at enzymatic and transcriptional levels. PLoS One 4:e7656 (2009). [PMID: 19888457]
5.	Kolos, I.K. and Makarchikov, A.F. [Identification of thiamine monophosphate hydrolyzing enzymes in chicken liver] Ukr. Biochem. J. 86 (2014) 39–49. [PMID: 25816604] (in Russian)
6.	Mimura, M., Zallot, R., Niehaus, T.D., Hasnain, G., Gidda, S.K., Nguyen, T.N., Anderson, E.M., Mullen, R.T., Brown, G., Yakunin, A.F., de Crecy-Lagard, V., Gregory, J.F., 3rd, McCarty, D.R. and Hanson, A.D. Arabidopsis TH₂ encodes the orphan enzyme thiamin monophosphate phosphatase. Plant Cell 28 (2016) 2683–2696. [PMID: 27677881]

[EC 3.1.3.100 created 2016]

3.1.3.101

Accepted name:

validoxylamine A 7′-phosphate phosphatase

Reaction:

validoxylamine A 7′-phosphate + H₂O = validoxylamine A + phosphate

Glossary:

validoxylamine A = (1S,2S,3R,6S)-4-(hydroxymethyl)-6-{[(1S,2S,3S,4R,5R)-2,3,4-trihydroxy-5-(hydroxymethyl)cyclohexyl]amino}cyclohex-4-ene-1,2,3-triol

Other name(s):

vldH (gene name)

Systematic name:

validoxylamine-A 7′-phosphate phosphohydrolase

Comments:

The enzyme, characterized from the bacterium Streptomyces hygroscopicus subsp. limoneus, is involved in the biosynthesis of the antifungal agent validamycin A.

References:

1.	Asamizu, S., Yang, J., Almabruk, K.H. and Mahmud, T. Pseudoglycosyltransferase catalyzes nonglycosidic C-N coupling in validamycin a biosynthesis. J. Am. Chem. Soc. 133 (2011) 12124–12135. [PMID: 21766819]

[EC 3.1.3.101 created 2016]

3.1.3.102

Accepted name:

FMN hydrolase

Reaction:

FMN + H₂O = riboflavin + phosphate

Other name(s):

FMN phosphatase; AtcpFHy1

Systematic name:

FMN phosphohydrolase

Comments:

Requires Mg²⁺. The enzyme, found in many isoforms purified from both bacteria and plants, is a member of the haloacid dehalogenase superfamily. Most of the isoforms have a wide substrate specificity [2], but isoforms specific for FMN also exist [3].

References:

1.	Sandoval, F.J. and Roje, S. An FMN hydrolase is fused to a riboflavin kinase homolog in plants. J. Biol. Chem. 280 (2005) 38337–38345. [PMID: 16183635]
2.	Kuznetsova, E., Proudfoot, M., Gonzalez, C.F., Brown, G., Omelchenko, M.V., Borozan, I., Carmel, L., Wolf, Y.I., Mori, H., Savchenko, A.V., Arrowsmith, C.H., Koonin, E.V., Edwards, A.M. and Yakunin, A.F. Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family. J. Biol. Chem. 281 (2006) 36149–36161. [PMID: 16990279]
3.	Rawat, R., Sandoval, F.J., Wei, Z., Winkler, R. and Roje, S. An FMN hydrolase of the haloacid dehalogenase superfamily is active in plant chloroplasts. J. Biol. Chem. 286 (2011) 42091–42098. [PMID: 22002057]

[EC 3.1.3.102 created 2016]

3.1.3.103

Accepted name:

3-deoxy-D-glycero-D-galacto-nonulopyranosonate 9-phosphatase

Reaction:

3-deoxy-D-glycero-D-galacto-non-2-ulopyranosonate 9-phosphate + H₂O = 3-deoxy-D-glycero-D-galacto-non-2-ulopyranosonate + phosphate

Other name(s):

3-deoxy-D-glycero-D-galacto-non-2-ulopyranosonate-9-phosphate phosphatase

Systematic name:

3-deoxy-D-glycero-D-galacto-non-2-ulopyranosonate 9-phosphohydrolase

Comments:

The enzyme, characterized from the bacterium Bacteroides thetaiotaomicron, is part of the biosynthesis pathway of the sialic acid 3-deoxy-D-glycero-D-galacto-non-2-ulopyranosonate (Kdn). Kdn is abundant in extracellular glycoconjugates of lower vertebrates such as fish and amphibians, but is also found in the capsular polysaccharides of bacteria that belong to the Bacteroides genus.

References:

1.	Wang, L., Lu, Z., Allen, K.N., Mariano, P.S. and Dunaway-Mariano, D. Human symbiont Bacteroides thetaiotaomicron synthesizes 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN). Chem. Biol. 15 (2008) 893–897. [PMID: 18804026]
2.	Lu, Z., Wang, L., Dunaway-Mariano, D. and Allen, K.N. Structure-function analysis of 2-keto-3-deoxy-D-glycero-D-galactonononate-9-phosphate phosphatase defines specificity elements in type C₀ haloalkanoate dehalogenase family members. J. Biol. Chem. 284 (2009) 1224–1233. [PMID: 18986982]

[EC 3.1.3.103 created 2016]

3.1.3.104

Accepted name:

5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase

Reaction:

5-amino-6-(5-phospho-D-ribitylamino)uracil + H₂O = 5-amino-6-(D-ribitylamino)uracil + phosphate

Other name(s):

5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5′-phosphate phosphatase

Systematic name:

5-amino-6-(5-phospho-D-ribitylamino)uracil phosphohydrolase

Comments:

Requires Mg²⁺. The enzyme, which is found in plants and bacteria, is part of a pathway for riboflavin biosynthesis. Most forms of the enzyme has a broad substrate specificity [1,3].

References:

1.	Haase, I., Sarge, S., Illarionov, B., Laudert, D., Hohmann, H.P., Bacher, A. and Fischer, M. Enzymes from the haloacid dehalogenase (HAD) superfamily catalyse the elusive dephosphorylation step of riboflavin biosynthesis. ChemBioChem 14 (2013) 2272–2275. [PMID: 24123841]
2.	London, N., Farelli, J.D., Brown, S.D., Liu, C., Huang, H., Korczynska, M., Al-Obaidi, N.F., Babbitt, P.C., Almo, S.C., Allen, K.N. and Shoichet, B.K. Covalent docking predicts substrates for haloalkanoate dehalogenase superfamily phosphatases. Biochemistry 54 (2015) 528–537. [PMID: 25513739]
3.	Sarge, S., Haase, I., Illarionov, B., Laudert, D., Hohmann, H.P., Bacher, A. and Fischer, M. Catalysis of an essential step in vitamin B₂ biosynthesis by a consortium of broad spectrum hydrolases. ChemBioChem 16 (2015) 2466–2469. [PMID: 26316208]

[EC 3.1.3.104 created 2016]

3.1.3.105

Accepted name:

N-acetyl-D-muramate 6-phosphate phosphatase

Reaction:

N-acetyl-D-muramate 6-phosphate + H₂O = N-acetyl-D-muramate + phosphate

Other name(s):

mupP (gene name)

Systematic name:

N-acetyl-D-muramate 6-phosphate phosphohydrolase

Comments:

The enzyme, characterized from Pseudomonas species, participates in a peptidoglycan salvage pathway.

References:

1.	Borisova, M., Gisin, J. and Mayer, C. The N-acetylmuramic acid 6-phosphate phosphatase MupP completes the Pseudomonas peptidoglycan recycling pathway leading to intrinsic fosfomycin resistance. mBio 8 (2017) e00092-17. [PMID: 28351914]

[EC 3.1.3.105 created 2017]

3.1.3.106

Accepted name:

2-lysophosphatidate phosphatase

Reaction:

a 1-acyl-sn-glycerol 3-phosphate + H₂O = a 1-acyl-sn-glycerol + phosphate

Other name(s):

1-acyl-sn-glycerol 3-phosphatase; CPC3 (gene name); PHM8 (gene name)

Systematic name:

1-acyl-sn-glycerol 3-phosphate phosphohydrolase

Comments:

The enzyme has been studied from the plants Arachis hypogaea (peanut) and Arabidopsis thaliana (thale cress) and from the yeast Saccharomyces cerevisiae. The enzyme from yeast, but not from the plants, requires Mg²⁺.

References:

1.	Shekar, S., Tumaney, A.W., Rao, T.J. and Rajasekharan, R. Isolation of lysophosphatidic acid phosphatase from developing peanut cotyledons. Plant Physiol. 128 (2002) 988–996. [PMID: 11891254]
2.	Reddy, V.S., Singh, A.K. and Rajasekharan, R. The Saccharomyces cerevisiae PHM8 gene encodes a soluble magnesium-dependent lysophosphatidic acid phosphatase. J. Biol. Chem. 283 (2008) 8846–8854. [PMID: 18234677]
3.	Reddy, V.S., Rao, D.K. and Rajasekharan, R. Functional characterization of lysophosphatidic acid phosphatase from Arabidopsis thaliana. Biochim. Biophys. Acta 1801 (2010) 455–461. [PMID: 20045079]

[EC 3.1.3.106 created 2019]

3.1.3.107

Accepted name:

amicoumacin phosphatase

Reaction:

amicoumacin A 2-phosphate + H₂O = amicoumacin A + phosphate

Other name(s):

amiO (gene name)

Systematic name:

amicoumacin 2-phosphate phosphohydrolase

Comments:

This bacterial enzyme activates the antibiotic amicoumacin A by removing a phosphate group that is added by EC 2.7.1.230, amicoumacin kinase.

References:

Terekhov, S.S., Smirnov, I.V., Malakhova, M.V., Samoilov, A.E., Manolov, A.I., Nazarov, A.S., Danilov, D.V., Dubiley, S.A., Osterman, I.A., Rubtsova, M.P., Kostryukova, E.S., Ziganshin, R.H., Kornienko, M.A., Vanyushkina, A.A., Bukato, O.N., Ilina, E.N., Vlasov, V.V., Severinov, K.V., Gabibov, A.G. and Altman, S. Ultrahigh-throughput functional profiling of microbiota communities. Proc. Natl. Acad. Sci. USA 115 (2018) 9551–9556. [PMID: 30181282]

[EC 3.1.3.107 created 2019]

3.1.3.108

Accepted name:

nocturnin

Reaction:

(1) NADPH + H₂O = NADH + phosphate
(2) NADP⁺ + H₂O = NAD⁺ + phosphate

Other name(s):

NOCT (gene name); nocturnin (curled); MJ0109 (gene name); NADP phosphatase; NADPase

Systematic name:

NADPH 2′-phosphohydrolase

Comments:

The mammalian mitochondrial enzyme is a rhythmically expressed protein that regulates metabolism under the control of circadian clock. It has a slight preference for NADPH over NADP⁺. The archaeal enzyme, identified in Methanocaldococcus jannaschii, is bifunctional acting as NAD⁺ kinase (EC 2.7.1.23) and NADP⁺ phosphatase with a slight preference for NADP⁺ over NADPH.

References:

1.	Kawai, S. and Murata, K. Structure and function of NAD kinase and NADP phosphatase: key enzymes that regulate the intracellular balance of NAD(H) and NADP(H). Biosci. Biotechnol. Biochem. 72 (2008) 919–930. [PMID: 18391451]
2.	Abshire, E.T., Chasseur, J., Bohn, J.A., Del Rizzo, P.A., Freddolino, P.L., Goldstrohm, A.C. and Trievel, R.C. The structure of human nocturnin reveals a conserved ribonuclease domain that represses target transcript translation and abundance in cells. Nucleic Acids Res. 46 (2018) 6257–6270. [PMID: 29860338]
3.	Estrella, M.A., Du, J. and Korennykh, A. Crystal structure of human nocturnin catalytic domain. Sci. Rep. 8:16294 (2018). [PMID: 30389976]
4.	Estrella, M.A., Du, J., Chen, L., Rath, S., Prangley, E., Chitrakar, A., Aoki, T., Schedl, P., Rabinowitz, J. and Korennykh, A. The metabolites NADP⁺ and NADPH are the targets of the circadian protein nocturnin (curled). Nat. Commun. 10:2367 (2019). [PMID: 31147539]

[EC 3.1.3.108 created 2020]

3.1.30.1

Accepted name:

Aspergillus nuclease S₁

Reaction:

Endonucleolytic cleavage to 5′-phosphomononucleotide and 5′-phosphooligonucleotide end-products

Other name(s):

endonuclease S₁ (Aspergillus); single-stranded-nucleate endonuclease; deoxyribonuclease S₁; deoxyribonuclease S₁; nuclease S₁; Neurospora crassa single-strand specific endonuclease; S1 nuclease; single-strand endodeoxyribonuclease; single-stranded DNA specific endonuclease; single-strand-specific endodeoxyribonuclease; single strand-specific DNase; Aspergillus oryzae S1 nuclease

References:

1.	Ando, T. A nuclease specific for heat-denatured DNA isolated from a product of Aspergillus oryzae. Biochim. Biophys. Acta 114 (1966) 158–168. [PMID: 4287053]
2.	Sutton, W.D. A crude nuclease preparation suitable for use in DNA reassociation experiments. Biochim. Biophys. Acta 240 (1971) 522–531. [PMID: 5123563]
3.	Vogt, V.M. Purification and further properties of single-strand-specific nuclease from Aspergillus oryzae. Eur. J. Biochem. 33 (1973) 192–200. [PMID: 4691350]

[EC 3.1.30.1 created 1972 as EC 3.1.4.21, transferred 1978 to EC 3.1.30.1, modified 1981]

3.1.30.2

Accepted name:

Serratia marcescens nuclease

Reaction:

Endonucleolytic cleavage to 5′-phosphomononucleotide and 5′-phosphooligonucleotide end-products

Other name(s):

endonuclease (Serratia marcescens); barley nuclease; plant nuclease I; nucleate endonuclease

Comments:

Hydrolyses double- or single-stranded substrate.

References:

1.	Mikulski, A.J. and Laskowski, M. , Sr. Mung bean nuclease I. 3. Purification procedure and (3′) ω monophosphatase activity. J. Biol. Chem. 245 (1970) 5026–5031. [PMID: 4319109]
2.	Stevens, A. and Hilmoe, R.J. Studies on a nuclease from Azotobacter agilis. I. Isolation and mode of action. J. Biol. Chem. 235 (1960) 3016–3022.
3.	Stevens, A. and Hilmoe, R.J. Studies on a nuclease from Azotobacter agilis. II. Hydrolysis of ribonucleic and deoxyribonucleic acids. J. Biol. Chem. 235 (1960) 3023–3027.
4.	Wechter, W.J., Mikulski, A.J. and Laskowski, M. , Sr. Gradation of specificity with regard to sugar among nucleases. Biochem. Biophys. Res. Commun. 30 (1968) 318–322. [PMID: 4296679]

[EC 3.1.30.2 created 1965 as EC 3.1.4.9, transferred 1978 to EC 3.1.30.2, modified 1981]

3.1.31.1

Accepted name:

micrococcal nuclease

Reaction:

Endonucleolytic cleavage to nucleoside 3′-phosphates and 3′-phosphooligonucleotide end-products

Other name(s):

spleen endonuclease; thermonuclease; nuclease T; micrococcal endonuclease; nuclease T′; staphylococcal nuclease; spleen phosphodiesterase; Staphylococcus aureus nuclease; Staphylococcus aureus nuclease B; ribonucleate (deoxynucleate) 3′-nucleotidohydrolase

Comments:

Hydrolyses double- or single-stranded substrate.

References:

1.	Alexander, M., Heppel, L.A. and Hurwitz, J. The purification and properties of micrococcal nuclease. J. Biol. Chem. 236 (1961) 3014–3019. [PMID: 13860347]
2.	Anfinsen, C.B., Cuatrecasas, P. and Taniuchi, H. Staphylococcal nuclease, chemical properties and catalysis. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 4, Academic Press, New York, 1971, pp. 177–204.
3.	Reddi, K.K. Micrococcal nuclease. Methods Enzymol. 12A (1967) 257–262.
4.	Sulkowski, E. and Laskowski, M. , Sr. Phosphatase-free crystalline micrococcal nuclease. J. Biol. Chem. 241 (1966) 4386–4388. [PMID: 5922962]

[EC 3.1.31.1 created 1961 as EC 3.1.4.7, transferred 1978 to EC 3.1.31.1, modified 1981]