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] |
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[EC 3.1.3.46 created 1984] |
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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] |
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[EC 3.1.3.47 created 1984] |
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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] |
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[EC 3.1.3.48 created 1984] |
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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] |
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[EC 3.1.3.49 created 1984] |
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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, PDB, 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. |
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[EC 3.1.3.50 created 1984] |
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EC |
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 |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 72994-50-4 |
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. [DOI] [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] |
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[EC 3.1.3.51 created 1984] |
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EC |
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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 87244-20-0, 88086-29-7 |
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. [DOI] [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. [DOI] [PMID: 3004826] |
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[EC 3.1.3.52 created 1986] |
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EC |
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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 60241-39-6 |
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] |
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[EC 3.1.3.53 created 1986] |
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EC |
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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 111684-53-8 |
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. [DOI] [PMID: 3036508] |
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[EC 3.1.3.54 created 1989] |
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EC |
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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 93229-71-1 |
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] |
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[EC 3.1.3.55 created 1989] |
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EC |
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 |
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For diagram of myo-inositol-phosphate biosynthesis, click here |
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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 106283-14-1 |
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. [DOI] [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] |
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[EC 3.1.3.56 created 1989, modified 2002] |
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EC |
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 |
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For diagram of myo-inositol-phosphate biosynthesis, click here |
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 Vmax 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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 111070-17-8, 111694-13-4 |
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] |
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[EC 3.1.3.57 created 1989, modified 2002] |
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EC |
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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 99283-70-2 |
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] |
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[EC 3.1.3.58 created 1989] |
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EC |
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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 102925-45-1 |
References: |
1. |
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] |
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[EC 3.1.3.59 created 1989] |
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EC |
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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 122319-89-5 |
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] |
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[EC 3.1.3.60 created 1992] |
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EC
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3.1.3.61
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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] |
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EC |
3.1.3.62 |
Accepted name: |
multiple inositol-polyphosphate phosphatase |
Reaction: |
(1) myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate (2) 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + H2O = 1D-myo-inositol 1,2,5,6-tetrakisphosphate + phosphate (3) 1D-myo-inositol 1,2,5,6-tetrakisphosphate + H2O = 1D-myo-inositol 1,2,6-trisphosphate + phosphate (4) 1D-myo-inositol 1,2,6-trisphosphate + H2O = 1D-myo-inositol 1,2-bisphosphate + phosphate (5) 1D-myo-inositol 1,2-bisphosphate + H2O = 1D-myo-inositol 2-phosphate + phosphate |
Glossary: |
myo-inositol hexakisphosphate = phytate
1D-myo-inositol 1,3,4,5,6-pentakisphosphate = Ins(1,3,4,5,6)P5
1D-myo-inositol 1,3,4,5-tetrakisphosphate = Ins(1,3,4,5)P4
1D-myo-inositol 1,4,5,6-tetrakisphosphate = Ins(1,4,5,6)P4
1D-myo-inositol 1,4,5-trisphosphate = Ins(1,4,5)P3
1D-myo-inositol 2,3-bisphosphate = Ins(2,3)P2
1D-myo-inositol 2-phosphate = Ins(2)P
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Other name(s): |
MIPP; phytase (ambiguous); 1D-myo-inositol-hexakisphosphate 5-phosphohydrolase (incorrect) |
Systematic name: |
myo-inositol-hexakisphosphate phosphohydrolase |
Comments: |
This ubiquitous enzyme degrades myo-inositol hexakisphosphate (phytate) to Ins(2,3)P2 and Ins(2)P. Activities have been characterized in the yeast Saccharomyces cerevisiae [2], the plant Lupinus albus [3] and the bacteria Bacillus sp. [4] and Raoultella terrigena [5]. In mammal cells Ins(2,3)P2 and Ins(2)P are the major inositol phosphate compounds found [6]. The mammal enzyme is also active on Ins(1,3,4,5,6)P5 that is dephosphorylated to Ins(1,4,5,6)P4 and Ins(1,4,5)P3, and on 2,3-bisphospho-D-glycerate (cf. EC 3.1.3.80, 2,3-bisphosphoglycerate 3-phosphatase). In addition, it acts on Ins(1,3,4,5)P4 to yield Ins(1,4,5)P3 in vitro (cf. EC 3.1.3.67, phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase) [7]. It does not hydrolyse phosphates from the 2-positions of inositol phosphates [6]. In other organisms the degradation of phytate follows different routes. (cf. EC 3.1.3.8, 3-phytase, EC 3.1.3.26, 4-phytase, and EC 3.1.3.72, 5-phytase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 116958-30-6 |
References: |
1. |
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. [DOI] [PMID: 9359836] |
2. |
Greiner, R., Alminger, M.L. and Carlsson, N.G. Stereospecificity of myo-inositol hexakisphosphate dephosphorylation by a phytate-degrading enzyme of baker’s yeast. J. Agric. Food Chem. 49 (2001) 2228–2233. [DOI] [PMID: 11368581] |
3. |
Greiner, R., Larsson Alminger, M., Carlsson, N.G., Muzquiz, M., Burbano, C., Cuadrado, C., Pedrosa, M.M. and Goyoaga, C. Pathway of dephosphorylation of myo-inositol hexakisphosphate by phytases of legume seeds. J. Agric. Food Chem. 50 (2002) 6865–6870. [DOI] [PMID: 12405789] |
4. |
Greiner, R., Farouk, A., Alminger, M.L. and Carlsson, N.G. The pathway of dephosphorylation of myo-inositol hexakisphosphate by phytate-degrading enzymes of different Bacillus spp. Can. J. Microbiol. 48 (2002) 986–994. [DOI] [PMID: 12556126] |
5. |
Greiner, R. and Carlsson, N.G. myo-Inositol phosphate isomers generated by the action of a phytate-degrading enzyme from Klebsiella terrigena on phytate. Can. J. Microbiol. 52 (2006) 759–768. [DOI] [PMID: 16917535] |
6. |
Nguyen Trung, M., Kieninger, S., Fandi, Z., Qiu, D., Liu, G., Mehendale, N.K., Saiardi, A., Jessen, H., Keller, B. and Fiedler, D. Stable isotopomers of myo-inositol uncover a complex MINPP1-dependent inositol phosphate network. ACS Cent. Sci. 8 (2022) 1683–1694. [DOI] [PMID: 36589890] |
7. |
Yu, J., Leibiger, B., Yang, S.N., Shears, S.B., Leibiger, I.B., Berggren, P.O. and Barker, C.J. Multiple inositol polyphosphate phosphatase compartmentalization separates inositol phosphate metabolism from inositol lipid signaling. Biomolecules 13 (2023) . [DOI] [PMID: 37371464] |
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[EC 3.1.3.62 created 1992, modified 2002, modified 2023] |
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EC |
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 |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 122319-88-4 |
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] |
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|
EC |
3.1.3.64 |
Accepted name: |
phosphatidylinositol-3-phosphatase |
Reaction: |
1-phosphatidyl-1D-myo-inositol 3-phosphate + H2O = 1-phosphatidyl-1D-myo-inositol + phosphate |
|
For diagram of 1-phosphatidyl-myo-inositol metabolism, click here |
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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 124248-47-1 |
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] |
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[EC 3.1.3.64 created 1992, [EC 3.1.3.65 created 1992, incorporated 2002], modified 2002]] |
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EC
|
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] |
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EC |
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 |
|
For diagram of 1-phosphatidyl-myo-inositol metabolism, click here |
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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 123644-80-4 |
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. [DOI] [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. [DOI] [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. [DOI] [PMID: 9295334] |
|
[EC 3.1.3.66 created 1992, modified 2002] |
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EC |
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 |
|
For diagram of 1-phosphatidyl-myo-inositol metabolism, click here |
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 (gene name); MMAC1 (gene name); 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 |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 210488-47-4 |
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. [DOI] [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. [DOI] [PMID: 9593664] |
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[EC 3.1.3.67 created 1999, modified 2002] |
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EC |
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 |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 65187-56-6 |
References: |
1. |
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. [DOI] [PMID: 8091229] |
2. |
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. [DOI] [PMID: 8553694] |
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[EC 3.1.3.68 created 1999] |
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EC |
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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 161515-14-6 |
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. [DOI] [PMID: 9045835] |
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[EC 3.1.3.69 created 2001, modified 2015] |
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EC |
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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 393512-74-8 |
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. [DOI] [PMID: 11562374] |
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[EC 3.1.3.70 created 2002] |
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EC |
3.1.3.71 |
Accepted name: |
2-phosphosulfolactate phosphatase |
Reaction: |
(2R)-2-phospho-3-sulfolactate + H2O = (2R)-3-sulfolactate + phosphate |
|
For diagram of coenzyme-M biosynthesis, click here |
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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 409095-18-7 |
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. [DOI] [PMID: 11589710] |
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[EC 3.1.3.71 created 2002] |
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EC |
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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 357208-41-4 |
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] |
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[EC 3.1.3.72 created 2002] |
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EC |
3.1.3.73 |
Accepted name: |
adenosylcobalamin/α-ribazole phosphatase |
Reaction: |
(1) adenosylcobalamin 5′-phosphate + H2O = adenosylcobalamin + phosphate (2) α-ribazole 5′-phosphate + H2O = α-ribazole + phosphate |
|
For diagram of corrin biosynthesis (part 8), click here |
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]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 251991-06-7 |
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. [DOI] [PMID: 17209023] |
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[EC 3.1.3.73 created 2004, modified 2011] |
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EC |
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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9076-92-0 |
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. [DOI] [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. [DOI] [PMID: 14522954] |
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[EC 3.1.3.74 created 2004] |
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EC |
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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
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. [DOI] [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. [DOI] [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. [DOI] [PMID: 15175005] |
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[EC 3.1.3.75 created 2004] |
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EC |
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]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 15096040] |
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[EC 3.1.3.76 created 2006] |
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EC |
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 |
|
For diagram of methionine salvage, click here |
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]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
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. [DOI] [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. [DOI] [PMID: 15843022] |
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[EC 3.1.3.77 created 2006] |
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|
|
EC |
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]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 17389247] |
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[EC 3.1.3.78 created 2008] |
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EC |
3.1.3.79 |
Accepted name: |
mannosylfructose-phosphate phosphatase |
Reaction: |
β-D-fructofuranosyl-α-D-mannopyranoside 6F-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 6F-phosphate is used to indicate that the fructose residue of sucrose carries the substituent. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
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. [DOI] [PMID: 17728402] |
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[EC 3.1.3.79 created 2009] |
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EC |
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). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
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. [DOI] [PMID: 18413611] |
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[EC 3.1.3.80 created 2010] |
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EC
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3.1.3.81
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Transferred entry: | diacylglycerol diphosphate phosphatase. Now EC 3.6.1.75, diacylglycerol diphosphate phosphatase
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[EC 3.1.3.81 created 2010, deleted 2022] |
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EC |
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
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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]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
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. [DOI] [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. [DOI] [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. [DOI] [PMID: 20050615] |
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[EC 3.1.3.82 created 2010] |
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EC |
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
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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]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
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. [DOI] [PMID: 20050615] |
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[EC 3.1.3.83 created 2010] |
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EC |
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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
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. [DOI] [PMID: 15684411] |
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[EC 3.1.3.84 created 2011] |
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EC |
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]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
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. [DOI] [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. [DOI] [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). [DOI] [PMID: 22355692] |
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[EC 3.1.3.85 created 2011] |
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EC |
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 |
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For diagram of 1-phosphatidyl-myo-inositol metabolism, click here |
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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 9824312] |
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[EC 3.1.3.86 created 2011] |
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EC |
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]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
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. [DOI] [PMID: 14551435] |
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[EC 3.1.3.87 created 2012] |
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EC |
3.1.3.88 |
Accepted name: |
5′′-phosphoribostamycin phosphatase |
Reaction: |
5′′-phosphoribostamycin + H2O = ribostamycin + phosphate |
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For diagram of neamine and ribostamycin biosynthesis, click here |
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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
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. [DOI] [PMID: 17482823] |
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[EC 3.1.3.88 created 2012] |
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EC |
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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
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. [DOI] [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. [DOI] [PMID: 18353368] |
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[EC 3.1.3.89 created 2013] |
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EC |
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). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
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. [DOI] [PMID: 23490043] |
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[EC 3.1.3.90 created 2013] |
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EC |
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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
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. [DOI] [PMID: 23223233] |
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[EC 3.1.3.91 created 2013] |
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EC |
3.1.3.92 |
Accepted name: |
kanosamine-6-phosphate phosphatase |
Reaction: |
kanosamine 6-phosphate + H2O = kanosamine + phosphate |
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For diagram of kanosamine biosynthesis, click here |
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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
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. [DOI] [PMID: 23586652] |
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[EC 3.1.3.92 created 2013] |
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EC |
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). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
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. [DOI] [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. [DOI] [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. [DOI] [PMID: 20023146] |
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[EC 3.1.3.93 created 2014] |
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EC |
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). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Parthasarathy, R., Parthasarathy, L. and Vadnal, R. Brain inositol monophosphatase identified as a galactose 1-phosphatase. Brain Res. 778 (1997) 99–106. [DOI] [PMID: 9462881] |
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[EC 3.1.3.94 created 2014] |
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EC |
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
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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). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
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. [DOI] [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. [DOI] [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] |
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[EC 3.1.3.95 created 2014] |
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