The Enzyme Database

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EC 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)
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9001-78-9
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. [DOI] [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. [DOI] [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. (Eds), The Enzymes, 2nd edn, vol. 5, Academic Press, New York, 1961, pp. 55–71.
[EC 3.1.3.1 created 1961]
 
 
EC 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.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9001-77-8
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. [DOI] [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]
 
 
EC 3.1.3.3     
Accepted name: phosphoserine phosphatase
Reaction: O-phospho-L(or D)-serine + H2O = L(or D)-serine + phosphate
For diagram of serine biosynthesis, click here
Systematic name: O-phosphoserine phosphohydrolase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9025-73-4
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. (Eds), 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]
 
 
EC 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9025-77-8
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. [DOI] [PMID: 18812320]
[EC 3.1.3.4 created 1961, modified 2010]
 
 
EC 3.1.3.5     
Accepted name: 5′-nucleotidase
Reaction: a 5′-ribonucleotide + H2O = a ribonucleoside + phosphate
For diagram of caffeine biosynthesis, click here
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.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9027-73-0
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]
 
 
EC 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9025-84-7
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]
 
 
EC 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9025-83-6
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. [DOI] [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. [DOI] [PMID: 179817]
[EC 3.1.3.7 created 1961]
 
 
EC 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
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-11-2
References:
1.  Cosgrove, D.J. Ion-exchange chromatography of inositol polyphosphates. Ann. N.Y. Acad. Sci. 165 (1969) 677–686. [DOI] [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. [DOI] [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]
 
 
EC 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)].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9001-39-2
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. [DOI] [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]
 
 
EC 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9001-38-1
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]
 
 
EC 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.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9001-52-9
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]
 
 
EC 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
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9025-72-3
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]
 
 
EC 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]
 
 
EC 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
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9025-78-9
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]
 
 
EC 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
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9025-79-0
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]
 
 
EC 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).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9025-75-6
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. [DOI] [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. [DOI] [PMID: 6092084]
[EC 3.1.3.16 created 1961, modified 1989, modified 2013]
 
 
EC 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
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9025-74-5
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. [DOI] [PMID: 13315351]
[EC 3.1.3.17 created 1961]
 
 
EC 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
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9025-76-7
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]
 
 
EC 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
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9027-39-8
References:
1.  Schmidt, G. Nonspecific acid phosphomonoesterases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds), 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]
 
 
EC 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
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9055-30-5
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]
 
 
EC 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37228-75-4
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]
 
 
EC 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
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9055-29-2
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]
 
 
EC 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9023-07-8
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]
 
 
EC 3.1.3.24     
Accepted name: sucrose-phosphate phosphatase
Reaction: sucrose 6F-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-6F-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 6F-phosphate is used to indicate that the fructose residue of sucrose carries the substituent.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9059-33-0
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-6F-phosphate phosphohydrolase from plants. Proc. Natl. Acad. Sci. USA 97 (2000) 12914–12919. [DOI] [PMID: 11050182]
3.  Lunn, J.E. and MacRae, E. New complexities in the synthesis of sucrose. Curr. Opin. Plant Biol. 6 (2003) 208–214. [DOI] [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. [DOI] [PMID: 15937230]
[EC 3.1.3.24 created 1972, modified 2008]
 
 
EC 3.1.3.25     
Accepted name: inositol-phosphate phosphatase
Reaction: myo-inositol phosphate + H2O = myo-inositol + phosphate
For diagram of myo-inositol biosynthesis, click here
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].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37184-63-7
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]
 
 
EC 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
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9001-89-2
References:
1.  Johnson, L.F. and Tate, M.E. The structure of myo-inositol pentaphosphates. Ann. N.Y. Acad. Sci. 165 (1969) 526–532. [DOI] [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. [DOI] [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]
 
 
EC 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
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9033-46-9
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]
 
 
EC 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37288-12-3
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]
 
 
EC 3.1.3.29     
Accepted name: N-acylneuraminate-9-phosphatase
Reaction: N-acylneuraminate 9-phosphate + H2O = N-acylneuraminate + phosphate
For diagram of N-Acetylneuraminic acid biosynthesis, click here
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
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-13-4
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]
 
 
EC 3.1.3.30      
Deleted entry:  3′-phosphoadenylylsulfate 3′-phosphatase. Now included with EC 3.1.3.31 nucleotidase
[EC 3.1.3.30 created 1972, deleted 1992]
 
 
EC 3.1.3.31     
Accepted name: nucleotidase
Reaction: a nucleotide + H2O = a nucleoside + phosphate
Other name(s): nucleotide phosphatase; nucleotide-specific phosphatase; NSP I; NSP II; deoxyribonucleoside-activated nucleotidase (DAN); deoxyinosine-activated nucleotidase (DIAN); acid nucleotidase
Systematic name: nucleotide phosphohydrolase
Comments: A wide specificity for 2′, 3′- and 5′- nucleotides; also hydrolyses glycerol phosphate and 4-nitrophenyl phosphate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9033-33-4
References:
1.  Arsenis, C. and Touster, O. Purification and properties of an acid nucleotidase from rat liver lysosomes. J. Biol. Chem. 243 (1968) 5702–5708. [PMID: 5699060]
[EC 3.1.3.31 created 1972 (EC 3.1.3.30 created 1972, incorporated 1992)]
 
 
EC 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-16-7
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]
 
 
EC 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-17-8
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]
 
 
EC 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37288-18-9
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]
 
 
EC 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9026-80-6
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]
 
 
EC 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
For diagram of 1-phosphatidyl-myo-inositol metabolism, click here
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9036-01-5
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. [DOI] [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]
 
 
EC 3.1.3.37     
Accepted name: sedoheptulose-bisphosphatase
Reaction: sedoheptulose 1,7-bisphosphate + H2O = sedoheptulose 7-phosphate + phosphate
For diagram of the Calvin cycle, click here
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
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9055-32-7
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. [DOI] [PMID: 4329855]
[EC 3.1.3.37 created 1976]
 
 
EC 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 62213-13-2
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]
 
 
EC 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9055-33-8
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]
 
 
EC 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
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9055-28-1
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]
 
 
EC 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9073-68-1
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. [DOI] [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. [DOI] [PMID: 4357666]
[EC 3.1.3.41 created 1976]
 
 
EC 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9043-28-1
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. [DOI] [PMID: 4367978]
[EC 3.1.3.42 created 1976]
 
 
EC 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9073-70-5
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. [DOI] [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]
 
 
EC 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}.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 77000-10-3
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]
 
 
EC 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
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 59088-24-3
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]
 
 
EC 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).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 81611-75-8
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. [DOI] [PMID: 6282585]
[EC 3.1.3.46 created 1984]
 
 
EC 3.1.3.47     
Accepted name: [hydroxymethylglutaryl-CoA reductase (NADPH)]-phosphatase
Reaction: [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate + H2O = [hydroxymethylglutaryl-CoA reductase (NADPH)] + phosphate
For diagram of mevalonate biosynthesis, click here
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).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 73507-97-8
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. [DOI] [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. [DOI] [PMID: 6260210]
[EC 3.1.3.47 created 1984]
 
 
EC 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 79747-53-8
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. [DOI] [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. [DOI] [PMID: 6273884]
[EC 3.1.3.48 created 1984]
 
 
EC 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 79986-25-7
References:
1.  Jett, M.-F., Hue, L. and Hers, H.-G. Pyruvate kinase phosphatase. FEBS Lett. 132 (1981) 183–186. [DOI] [PMID: 6271587]
[EC 3.1.3.49 created 1984]
 
 
EC 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 80449-21-4
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]
 
 


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