Enzyme Nomenclature

EC 3.1.3 (continued)

Phosphoric Monoester Hydrolases

Continued from EC 3.1.3.1 to EC 3.1.3.50

Contents

EC 3.1.3.51 dolichyl-phosphatase
EC 3.1.3.52 [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]-phosphatase
EC 3.1.3.53 [myosin-light-chain] phosphatase
EC 3.1.3.54 fructose-2,6-bisphosphate 6-phosphatase
EC 3.1.3.55 caldesmon-phosphatase
EC 3.1.3.56 inositol-polyphosphate 5-phosphatase
EC 3.1.3.57 inositol-1,4-bisphosphate 1-phosphatase
EC 3.1.3.58 sugar-terminal-phosphatase
EC 3.1.3.59 alkylacetylglycerophosphatase
EC 3.1.3.60 phosphoenolpyruvate phosphatase
EC 3.1.3.61 deleted
EC 3.1.3.62 multiple inositol-polyphosphate phosphatase
EC 3.1.3.63 2-carboxy-D-arabinitol-1-phosphatase
EC 3.1.3.64 phosphatidylinositol-3-phosphatase
EC 3.1.3.65 now with EC 3.1.3.64
EC 3.1.3.66 phosphatidylinositol-3,4-bisphosphate 4-phosphatase
EC 3.1.3.67 phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase
EC 3.1.3.68 2-deoxyglucose-6-phosphatase
EC 3.1.3.69 glucosylglycerol 3-phosphatase
EC 3.1.3.70 mannosyl-3-phosphoglycerate phosphatase
EC 3.1.3.71 2-phosphosulfolactate phosphatase
EC 3.1.3.72 5-phytase
EC 3.1.3.73 adenosylcobalamin/α-ribazole phosphatase
EC 3.1.3.74 pyridoxal phosphatase
EC 3.1.3.75 phosphoethanolamine/phosphocholine phosphatase
EC 3.1.3.76 lipid-phosphate phosphatase
EC 3.1.3.77 acireductone synthase
EC 3.1.3.78 phosphatidylinositol-4,5-bisphosphate 4-phosphatase
EC 3.1.3.79 mannosylfructose-phosphate phosphatase
EC 3.1.3.80 2,3-bisphosphoglycerate 3-phosphatase
EC 3.1.3.81 diacylglycerol diphosphate phosphatase
EC 3.1.3.82 D-glycero-β-D-manno-heptose 1,7-bisphosphate 7-phosphatase
EC 3.1.3.83 D-glycero-α-D-manno-heptose 1,7-bisphosphate 7-phosphatase
EC 3.1.3.84 ADP-ribose 1"-phosphate phosphatase
EC 3.1.3.85 glucosyl-3-phosphoglycerate phosphatase
EC 3.1.3.86 phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase
EC 3.1.3.87 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase
EC 3.1.3.88 5"-phosphoribostamycin phosphatase
EC 3.1.3.89 5'-deoxynucleotidase
EC 3.1.3.90 maltose 6'-phosphate phosphatase
EC 3.1.3.91 7-methylguanosine nucleotidase
EC 3.1.3.92 kanosamine-6-phosphate phosphatase
EC 3.1.3.93 L-galactose 1-phosphate phosphatase
EC 3.1.3.94 D-galactose 1-phosphate phosphatase
EC 3.1.3.95 phosphatidylinositol-3,5-bisphosphate 3-phosphatase
EC 3.1.3.96 pseudouridine 5'-phosphatase
EC 3.1.3.97 3',5'-nucleoside bisphosphate phosphatase
EC 3.1.3.98 now EC 3.6.1.68
EC 3.1.3.99 IMP-specific 5'-nucleotidase
EC 3.1.3.100 thiamine phosphate phosphatase
EC 3.1.3.101 validoxylamine A 7'-phosphate phosphatase
EC 3.1.3.102 FMN hydrolase
EC 3.1.3.103 3-deoxy-D-glycero-D-galacto-nononate 9-phosphatase
EC 3.1.3.104 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase
EC 3.1.3.105 N-acetyl-D-muramate 6-phosphate phosphatase

Entries

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. [PMID: 229909]

2. Rip, J.W., Rupar, C.A., Chaudhary, N. and Carroll, K.K. Localization of a dolichyl phosphate phosphatase in plasma membranes of rat liver. J. Biol. Chem. 256 (1981) 1929-1934. [PMID: 6257694]

3. Wedgwood, J.F. and Strominger, J.L. Enzymatic activities in cultured human lymphocytes that dephosphorylate dolichyl pyrophosphate and dolichyl phosphate. J. Biol. Chem. 255 (1980) 1120-1123. [PMID: 6243292]

[EC 3.1.3.51 created 1984]

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; [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 and 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. [PMID: 6307746]

2. Reed, L.J., Damuni, Z. and Merryfield, M.L. Regulation of mammalian pyruvate and branched-chain α-keto acid dehydrogenase complexes by phosphorylation-dephosphorylation. Curr. Top. Cell. Regul. 27 (1985) 41-49. [PMID: 3004826]

[EC 3.1.3.52 created 1986]

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]

[EC 3.1.3.53 created 1986]

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. [PMID: 3036508]

[EC 3.1.3.54 created 1989]

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]

[EC 3.1.3.55 created 1989]

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

For diagram 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, 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. [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, Oxford University Press, Oxford, 2000, pp. 320-338.

4. Verjans, B., De Smedt, F., Lecocq, R., Vanweyenberg, V., Moreau, C. and Erneux, C. Cloning and expression in Escherichia coli of a dog thyroid cDNA encoding a novel inositol 1,4,5-trisphosphate 5-phosphatase. Biochem. J. 300 (1994) 85-90. [PMID: 8198557]

[EC 3.1.3.56 created 1989, modified 2002]

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

For diagram 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]

[EC 3.1.3.57 created 1989, modified 2002]

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]

[EC 3.1.3.58 created 1989]

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]

[EC 3.1.3.59 created 1989]

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, 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.

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.

[EC 3.1.3.60 created 1992]

[EC 3.1.3.61 Deleted entry: inositol-1,4,5-trisphosphate 1-phosphatase, as its existence has not been established (EC 3.1.3.61 created 1992, deleted 2002)]

EC 3.1.3.62

Accepted name: multiple inositol-polyphosphate phosphatase

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

Other name(s): inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase; inositol 1,3,4,5-tetrakisphosphate 3-phosphomonoesterase; inositol 1,3,4,5-tetrakisphosphate-5-phosphomonoesterase; inositol tetrakisphosphate phosphomonoesterase; inositol-1,3,4,5-tetrakisphosphate 3-phosphatase; MIPP

Systematic name: 1D-myo-inositol-hexakisphosphate 5-phosphohydrolase

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

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 116958-30-6

References:

1. Cullen, P.J., Irvine, R.F., Drøbak, B.J. and Dawson, A.P. Inositol 1,3,4,5-tetrakisphosphate causes release of Ca2+ from permeabilized mouse lymphoma L1210 cells by its conversion into inositol 1,4,5-trisphosphate. Biochem. J. 259 (1989) 931-933. [PMID: 2786415]

2. Craxton, A., Caffrey, J.J., Burkhart, W., Safrany, S.T. and Shears, S.B. Molecular cloning and expression of a rat hepatic multiple inositol polyphosphate phosphatase. Biochem. J. 328 (1997) 75-81. [PMID: 9359836]

[EC 3.1.3.62 created 1992, modified 2002]

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.

[EC 3.1.3.63 created 1992]

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 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]

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

[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)]

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 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; D-myo-inositol-3,4-bisphosphate 4-phosphohydrolase; 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. [PMID: 2546770]

2. Norris, F.A., Auethavekiat, V. and Majerus, P.W. The isolation and characterization of cDNA encoding human and rat brain inositol polyphosphate 4-phosphatase. J. Biol. Chem. 270 (1995) 16128-16133. [PMID: 7608176]

3. Norris, F.A., Atkins, R.C. and Majerus, P.W. The cDNA cloning and characterization of inositol polyphosphate 4-phosphatase type II. Evidence for conserved alternative splicing in the 4-phosphatase family. J. Biol. Chem. 272 (1997) 23859-23864. [PMID: 9295334]

[EC 3.1.3.66 created 1992, modified 2002]

EC 3.1.3.67

Accepted name: phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase

Reaction: phosphatidylinositol 3,4,5-trisphosphate + H2O = phosphatidylinositol 4,5-bisphosphate + phosphate

For diagram 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, MMAC1; phosphatidylinositol-3,4,5-trisphosphate 3-phosphohydrolase

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

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

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. [PMID: 8681945]

2. Maehama, T. and Dixon, J.E. The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. J. Biol. Chem. 273 (1998) 13375-13378. [PMID: 9593664]

[EC 3.1.3.67 created 1999, modified 2002]

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., Mardis, E., Menezes, S., Mouser, L., Nhan, M., Rifkin, L., Riles, L., St.Peter, H., Trevaskis, E., Vaughan, K., Vignati, D., Wilcox, L., Wohldman, P., Waterston, R., Wilson, R., Vaudin, M. Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII. Science 265 (1994) 2077-2082. [PMID: 8091229]

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. [PMID: 8553694]

[EC 3.1.3.68 created 1999]

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. [PMID: 9045835]

[EC 3.1.3.69 created 2001, modified 2015]

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. [PMID: 11562374]

[EC 3.1.3.70 created 2002]

EC 3.1.3.71

Accepted name: 2-phosphosulfolactate phosphatase

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

For diagram of reaction 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 hydrolyze 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. [PMID: 11589710]

[EC 3.1.3.71 created 2002]

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, 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]

[EC 3.1.3.72 created 2002]

EC 3.1.3.73

Accepted name: adenosylcobalamin/α-ribazole phosphatase

Reaction: (1) adenosylcobalamin 5'-phosphate + H2O = coenzyme B12 + phosphate
(2) α-ribazole 5'-phosphate + H2O = α-ribazole + phosphate

For diagram of the reaction 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, 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. [PMID: 17209023]

[EC 3.1.3.73 created 2004, modified 2011]

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. [PMID: 7625842]

3. Jang, Y.M., Kim, D.W., Kang, T.C., Won, M.H., Baek, N.I., Moon, B.J., Choi, S.Y. and Kwon, O.S. Human pyridoxal phosphatase. Molecular cloning, functional expression, and tissue distribution. J. Biol. Chem. 278 (2003) 50040-50046. [PMID: 14522954]

[EC 3.1.3.74 created 2004]

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, CAS registry number:

References:

1. Houston, B., Seawright, E., Jefferies, D., Hoogland, E., Lester, D., Whitehead, C. and Farquharson, C. Identification and cloning of a novel phosphatase expressed at high levels in differentiating growth plate chondrocytes. Biochim. Biophys. Acta 1448 (1999) 500-506. [PMID: 9990301]

2. Stewart, A.J., Schmid, R., Blindauer, C.A., Paisey, S.J. and Farquharson, C. Comparative modelling of human PHOSPHO1 reveals a new group of phosphatases within the haloacid dehalogenase superfamily. Protein Eng. 16 (2003) 889-895. [PMID: 14983068]

3. Roberts, S.J., Stewart, A.J., Sadler, P.J. and Farquharson C. Human PHOSPHO1 displays high specific phosphoethanolamine and phosphocholine phosphatase activities. Biochem. J. 382 (2004) 59-65. [PMID: 15175005]

[EC 3.1.3.75 created 2004]

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, CAS registry number:

References:

1. Newman, J.W., Morisseau, C., Harris, T.R. and Hammock, B.D. The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity. Proc. Natl. Acad. Sci. USA 100 (2003) 1558-1563. [PMID: 12574510]

2. Cronin, A., Mowbray, S., Durk, H., Homburg, S., Fleming, I., Fisslthaler, B., Oesch, F. and Arand, M. The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase. Proc. Natl. Acad. Sci. USA 100 (2003) 1552-1557. [PMID: 12574508]

3. Morisseau, C. and Hammock, B.D. Epoxide hydrolases: mechanisms, inhibitor designs, and biological roles. Annu. Rev. Pharmacol. Toxicol. 45 (2005) 311-333. [PMID: 15822179]

4. Tran, K.L., Aronov, P.A., Tanaka, H., Newman, J.W., Hammock, B.D. and Morisseau, C. Lipid sulfates and sulfonates are allosteric competitive inhibitors of the N-terminal phosphatase activity of the mammalian soluble epoxide hydrolase. Biochemistry 44 (2005) 12179-12187. [PMID: 16142916]

5. Newman, J.W., Morisseau, C. and Hammock, B.D. Epoxide hydrolases: their roles and interactions with lipid metabolism. Prog. Lipid Res. 44 (2005) 1-51. [PMID: 15748653]

6. Srivastava, P.K., Sharma, V.K., Kalonia, D.S. and Grant, D.F. Polymorphisms in human soluble epoxide hydrolase: effects on enzyme activity, enzyme stability, and quaternary structure. Arch. Biochem. Biophys. 427 (2004) 164-169. [PMID: 15196990]

7. Gomez, G.A., Morisseau, C., Hammock, B.D. and Christianson, D.W. Structure of human epoxide hydrolase reveals mechanistic inferences on bifunctional catalysis in epoxide and phosphate ester hydrolysis. Biochemistry 43 (2004) 4716-4723. [PMID: 15096040]

[EC 3.1.3.76 created 2006]

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 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, CAS registry number:

References:

1. Myers, R.W., Wray, J.W., Fish, S. and Abeles, R.H. Purification and characterization of an enzyme involved in oxidative carbon-carbon bond cleavage reactions in the methionine salvage pathway of Klebsiella pneumoniae. J. Biol. Chem. 268 (1993) 24785-24791. [PMID: 8227039]

2. Wray, J.W. and Abeles, R.H. The methionine salvage pathway in Klebsiella pneumoniae and rat liver. Identification and characterization of two novel dioxygenases. J. Biol. Chem. 270 (1995) 3147-3153. [PMID: 7852397]

[EC 3.1.3.77 created 2006]

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

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, CAS registry number:

References:

1. Niebuhr, K., Giuriato, S., Pedron, T., Philpott, D.J., Gaits, F., Sable, J., Sheetz, M.P., Parsot, C., Sansonetti, P.J. and Payrastre, B. Conversion of PtdIns(4,5)P2 into PtdIns(5)P by the S. flexneri effector IpgD reorganizes host cell morphology. EMBO J. 21 (2002) 5069-5078. [PMID: 12356723]

2. Ungewickell, A., Hugge, C., Kisseleva, M., Chang, S.C., Zou, J., Feng, Y., Galyov, E.E., Wilson, M. and Majerus, P.W. The identification and characterization of two phosphatidylinositol-4,5-bisphosphate 4-phosphatases. Proc. Natl. Acad. Sci. USA 102 (2005) 18854-18859. [PMID: 16365287]

3. Zou, J., Marjanovic, J., Kisseleva, M.V., Wilson, M. and Majerus, P.W. Type I phosphatidylinositol-4,5-bisphosphate 4-phosphatase regulates stress-induced apoptosis. Proc. Natl. Acad. Sci. USA 104 (2007) 16834-16839. [PMID: 17940011]

4. Mason, D., Mallo, G.V., Terebiznik, M.R., Payrastre, B., Finlay, B.B., Brumell, J.H., Rameh, L. and Grinstein, S. Alteration of epithelial structure and function associated with PtdIns(4,5)P2 degradation by a bacterial phosphatase. J. Gen. Physiol. 129 (2007) 267-283. [PMID: 17389247]

[EC 3.1.3.78 created 2008]

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, CAS registry number:

References:

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

[EC 3.1.3.79 created 2009]

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 3.1.3.13/EC 5.4.2.12 [phosphoglycerate mutase (2,3-diphosphoglycerate-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, CAS registry number:

References:

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

[EC 3.1.3.80 created 2010]

EC 3.1.3.81

Accepted name: diacylglycerol diphosphate phosphatase

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

Other name(s): DGPP phosphatase; DGPP phosphohydrolase; DPP1; DPPL1; DPPL2; PAP2; pyrophosphate phosphatase

Systematic name: 1,2-diacyl-sn-glycerol 3-phosphate phosphohydrolase

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

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Dillon, D.A., Wu, W.I., Riedel, B., Wissing, J.B., Dowhan, W. and Carman, G.M. The Escherichia coli pgpB gene encodes for a diacylglycerol pyrophosphate phosphatase activity. J. Biol. Chem. 271 (1996) 30548-30553. [PMID: 8940025]

2. Dillon, D.A., Chen, X., Zeimetz, G.M., Wu, W.I., Waggoner, D.W., Dewald, J., Brindley, D.N. and Carman, G.M. Mammalian Mg2+-independent phosphatidate phosphatase (PAP2) displays diacylglycerol pyrophosphate phosphatase activity. J. Biol. Chem. 272 (1997) 10361-10366. [PMID: 9099673]

3. Wu, W.I., Liu, Y., Riedel, B., Wissing, J.B., Fischl, A.S. and Carman, G.M. Purification and characterization of diacylglycerol pyrophosphate phosphatase from Saccharomyces cerevisiae. J. Biol. Chem. 271 (1996) 1868-1876. [PMID: 8567632]

4. Oshiro, J., Han, G.S. and Carman, G.M. Diacylglycerol pyrophosphate phosphatase in Saccharomyces cerevisiae. Biochim. Biophys. Acta 1635 (2003) 1-9. [PMID: 14642771]

5. Carman, G.M. Phosphatidate phosphatases and diacylglycerol pyrophosphate phosphatases in Saccharomyces cerevisiae and Escherichia coli. Biochim. Biophys. Acta 1348 (1997) 45-55. [PMID: 9370315]

6. Han, G.S., Johnston, C.N., Chen, X., Athenstaedt, K., Daum, G. and Carman, G.M. Regulation of the Saccharomyces cerevisiae DPP1-encoded diacylglycerol pyrophosphate phosphatase by zinc. J. Biol. Chem. 276 (2001) 10126-10133. [PMID: 11139591]

[EC 3.1.3.81 created 2010]

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

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, CAS registry number:

References:

1. Kneidinger, B., Marolda, C., Graninger, M., Zamyatina, A., McArthur, F., Kosma, P., Valvano, M.A. and Messner, P. Biosynthesis pathway of ADP-L-glycero-β-D-manno-heptose in Escherichia coli. J. Bacteriol. 184 (2002) 363-369. [PMID: 11751812]

2. Valvano, M.A., Messner, P. and Kosma, P. Novel pathways for biosynthesis of nucleotide-activated glycero-manno-heptose precursors of bacterial glycoproteins and cell surface polysaccharides. Microbiology 148 (2002) 1979-1989. [PMID: 12101286]

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

[EC 3.1.3.82 created 2010]

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

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, CAS registry number:

References:

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

[EC 3.1.3.83 created 2010]

EC 3.1.3.84

Accepted name: ADP-ribose 1"-phosphate phosphatase

Reaction: ADP-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-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, CAS registry number:

References:

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

[EC 3.1.3.84 created 2011]

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, CAS registry number:

References:

1. Costa, J., Empadinhas, N. and da Costa, M.S. Glucosylglycerate biosynthesis in the deepest lineage of the bacteria: characterization of the thermophilic proteins GpgS and GpgP from Persephonella marina. J. Bacteriol. 189 (2007) 1648-1654. [PMID: 17189358]

2. Costa, J., Empadinhas, N., Goncalves, L., Lamosa, P., Santos, H. and da Costa, M.S. Characterization of the biosynthetic pathway of glucosylglycerate in the archaeon Methanococcoides burtonii. J. Bacteriol. 188 (2006) 1022-1030. [PMID: 16428406]

[EC 3.1.3.85 created 2011]

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

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 hydroylses phosphatidylinositol-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, CAS registry number:

References:

1. Lioubin, M.N., Algate, P.A., Tsai, S., Carlberg, K., Aebersold, A. and Rohrschneider, L.R. p150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity. Genes Dev. 10 (1996) 1084-1095. [PMID: 8654924]

2. Damen, J.E., Liu, L., Rosten, P., Humphries, R.K., Jefferson, A.B., Majerus, P.W. and Krystal, G. The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-triphosphate 5-phosphatase. Proc. Natl. Acad. Sci. USA 93 (1996) 1689-1693. [PMID: 8643691]

3. Giuriato, S., Payrastre, B., Drayer, A.L., Plantavid, M., Woscholski, R., Parker, P., Erneux, C. and Chap, H. Tyrosine phosphorylation and relocation of SHIP are integrin-mediated in thrombin-stimulated human blood platelets. J. Biol. Chem. 272 (1997) 26857-26863. [PMID: 9341117]

4. Drayer, A.L., Pesesse, X., De Smedt, F., Woscholski, R., Parker, P. and Erneux, C. Cloning and expression of a human placenta inositol 1,3,4,5-tetrakisphosphate and phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase. Biochem. Biophys. Res. Commun. 225 (1996) 243-249. [PMID: 8769125]

5. Pesesse, X., Moreau, C., Drayer, A.L., Woscholski, R., Parker, P. and Erneux, C. The SH2 domain containing inositol 5-phosphatase SHIP2 displays phosphatidylinositol 3,4,5-trisphosphate and inositol 1,3,4,5-tetrakisphosphate 5-phosphatase activity. FEBS Lett. 437 (1998) 301-303. [PMID: 9824312]

[EC 3.1.3.86 created 2011]

EC 3.1.3.87

Accepted name: 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase

Reaction: 2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl 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

Systematic name: 2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl 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, CAS registry number:

References:

1. Myers, R.W., Wray, J.W., Fish, S. and Abeles, R.H. Purification and characterization of an enzyme involved in oxidative carbon-carbon bond cleavage reactions in the methionine salvage pathway of Klebsiella pneumoniae. J. Biol. Chem. 268 (1993) 24785-24791. [PMID: 8227039]

2. Ashida, H., Saito, Y., Kojima, C., Kobayashi, K., Ogasawara, N. and Yokota, A. A functional link between RuBisCO-like protein of Bacillus and photosynthetic RuBisCO. Science 302 (2003) 286-290. [PMID: 14551435]

[EC 3.1.3.87 created 2012]

EC 3.1.3.88

Accepted name: 5"-phosphoribostamycin phosphatase

Reaction: 5"-phosphoribostamycin + H2O = ribostamycin + phosphate

For diagram of reaction 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, CAS registry number:

References:

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

[EC 3.1.3.88 created 2012]

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, GTD, KEGG, CAS registry number:

References:

1. Proudfoot, M., Kuznetsova, E., Brown, G., Rao, N.N., Kitagawa, M., Mori, H., Savchenko, A. and Yakunin, A.F. General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG. J. Biol. Chem. 279 (2004) 54687-54694. [PMID: 15489502]

2. Zimmerman, M.D., Proudfoot, M., Yakunin, A. and Minor, W. Structural insight into the mechanism of substrate specificity and catalytic activity of an HD-domain phosphohydrolase: the 5'-deoxyribonucleotidase YfbR from Escherichia coli. J. Mol. Biol. 378 (2008) 215-226. [PMID: 18353368]

[EC 3.1.3.89 created 2013]

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, CAS registry number:

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. [PMID: 23490043]

[EC 3.1.3.90 created 2013]

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, CAS registry number:

References:

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

[EC 3.1.3.91 created 2013]

EC 3.1.3.92

Accepted name: kanosamine-6-phosphate phosphatase

Reaction: kanosamine 6-phosphate + H2O = kanosamine + phosphate

For diagram of reaction 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, CAS registry number:

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. [PMID: 23586652]

[EC 3.1.3.92 created 2013]

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, CAS registry number:

References:

1. Laing, W.A., Bulley, S., Wright, M., Cooney, J., Jensen, D., Barraclough, D. and MacRae, E. A highly specific L-galactose-1-phosphate phosphatase on the path to ascorbate biosynthesis. Proc. Natl. Acad. Sci. USA 101 (2004) 16976-16981. [PMID: 15550539]

2. Torabinejad, J., Donahue, J.L., Gunesekera, B.N., Allen-Daniels, M.J. and Gillaspy, G.E. VTC4 is a bifunctional enzyme that affects myoinositol and ascorbate biosynthesis in plants. Plant Physiol. 150 (2009) 951-961. [PMID: 19339506]

3. Petersen, L.N., Marineo, S., Mandala, S., Davids, F., Sewell, B.T. and Ingle, R.A. The missing link in plant histidine biosynthesis: Arabidopsis myoinositol monophosphatase-like2 encodes a functional histidinol-phosphate phosphatase. Plant Physiol. 152 (2010) 1186-1196. [PMID: 20023146]

[EC 3.1.3.93 created 2014]

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, CAS registry number:

References:

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

[EC 3.1.3.94 created 2014]

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

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, CAS registry number:

References:

1. Walker, D.M., Urbe, S., Dove, S.K., Tenza, D., Raposo, G. and Clague, M.J. Characterization of MTMR3. an inositol lipid 3-phosphatase with novel substrate specificity. Curr. Biol. 11 (2001) 1600-1605. [PMID: 11676921]

2. Berger, P., Bonneick, S., Willi, S., Wymann, M. and Suter, U. Loss of phosphatase activity in myotubularin-related protein 2 is associated with Charcot-Marie-Tooth disease type 4B1. Hum. Mol. Genet. 11 (2002) 1569-1579. [PMID: 12045210]

3. Ding, Y., Lapko, H., Ndamukong, I., Xia, Y., Al-Abdallat, A., Lalithambika, S., Sadder, M., Saleh, A., Fromm, M., Riethoven, J.J., Lu, G. and Avramova, Z. The Arabidopsis chromatin modifier ATX1, the myotubularin-like AtMTM and the response to drought. Plant Signal Behav 4 (2009) 1049-1058. [PMID: 19901554]

[EC 3.1.3.95 created 2014]

EC 3.1.3.96

Accepted name: pseudouridine 5'-phosphatase

Reaction: pseudouridine 5'-phosphate + H2O = pseudouridine + phosphate

Other name(s): pseudouridine 5'-monophosphatase; 5'-PsiMPase; HDHD1

Systematic name: pseudouridine 5'-phosphohydrolase

Comments: Requires Mg2+ for activity.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

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

[EC 3.1.3.96 created 2014]

EC 3.1.3.97

Accepted name: 3',5'-nucleoside bisphosphate phosphatase

Reaction: nucleoside 3',5'-bisphosphate + H2O = nucleoside 5'-phosphate + phosphate

Systematic name: nucleoside-3',5'-bisphosphate 3'-phosphohydrolase

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

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

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

[EC 3.1.3.97 created 2015]

[EC 3.1.3.98 Transferred entry: geranyl diphosphate phosphohydrolase, transferred to EC 3.6.1.68, geranyl diphosphate phosphohydrolase (EC 3.1.3.98 created 2015, deleted 2016)]

EC 3.1.3.99

Accepted name: IMP-specific 5'-nucleotidase

Reaction: IMP + H2O = inosine + phosphate

Other name(s): ISN1 (gene name)

Systematic name: inosine 5'-phosphate phosphohydrolase

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

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Itoh, R. Purification and some properties of an IMP-specific 5'-nucleotidase from yeast. Biochem. J. 298 (1994) 593-598. [PMID: 8141771]

2. Itoh, R., Saint-Marc, C., Chaignepain, S., Katahira, R., Schmitter, J.M. and Daignan-Fornier, B. The yeast ISN1 (YOR155c) gene encodes a new type of IMP-specific 5'-nucleotidase. BMC Biochem. 4 (2003) 4. [PMID: 12735798]

[EC 3.1.3.99 created 2016]

EC 3.1.3.100

Accepted name: thiamine phosphate phosphatase

Reaction: thiamine phosphate + H2O = thiamine + phosphate

Systematic name: thiamine phosphate phosphohydrolase

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

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Sanemori, H., Egi, Y. and Kawasaki, T. Pathway of thiamine pyrophosphate synthesis in Micrococcus denitrificans, J. Bacteriol. 126 (1976) 1030-1036. [PMID: 181359]

2. Komeda, Y., Tanaka, M. and Nishimune, T. A th-1 mutant of Arabidopsis thaliana is defective for a thiamin-phosphate-synthesizing enzyme: thiamin phosphate pyrophosphorylase. Plant Physiol. 88 (1988) 248-250. [PMID: 16666289]

3. Schweingruber, A.M., Dlugonski, J., Edenharter, E. and Schweingruber, M.E. Thiamine in Schizosaccharomyces pombe: dephosphorylation, intracellular pool, biosynthesis and transport. Curr. Genet. 19 (1991) 249-254. [PMID: 1868574]

4. Muller, I.B., Bergmann, B., Groves, M.R., Couto, I., Amaral, L., Begley, T.P., Walter, R.D. and Wrenger, C. The vitamin B1 metabolism of Staphylococcus aureus is controlled at enzymatic and transcriptional levels. PLoS One 4 (2009) e7656. [PMID: 19888457]

5. Kolos, I.K. and Makarchikov, A.F. [Identification of thiamine monophosphate hydrolyzing enzymes in chicken liver] Ukr Biochem J 86 (2014) 39-49. [PMID: 25816604] (in Russian)

6. Mimura, M., Zallot, R., Niehaus, T.D., Hasnain, G., Gidda, S.K., Nguyen, T.N., Anderson, E.M., Mullen, R.T., Brown, G., Yakunin, A.F., de Crecy-Lagard, V., Gregory, J.F., McCarty, D.R. and Hanson, A.D. Arabidopsis TH2 encodes the orphan enzyme thiamin monophosphate phosphatase. LID - tpc.00600.2016 [pii. Plant Cell 28 (2016) 2683-2696. [PMID: 27677881]

[EC 3.1.3.100 created 2016]

EC 3.1.3.101

Accepted name: validoxylamine A 7'-phosphate phosphatase

Reaction: validoxylamine A 7'-phosphate + H2O = validoxylamine A + phosphate

For diagram of reaction click here.

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

Other name(s): vldH (gene name)

Systematic name: validoxylamine-A 7'-phosphate phosphohydrolase

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

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

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

[EC 3.1.3.101 created 2016]

EC 3.1.3.102

Accepted name: FMN hydrolase

Reaction: FMN + H2O = riboflavin + phosphate

Other name(s): FMN phosphatase; AtcpFHy1

Systematic name: FMN phosphohydrolase

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

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Sandoval, F.J. and Roje, S. An FMN hydrolase is fused to a riboflavin kinase homolog in plants. J. Biol. Chem. 280 (2005) 38337-38345. [PMID: 16183635]

2. Kuznetsova, E., Proudfoot, M., Gonzalez, C.F., Brown, G., Omelchenko, M.V., Borozan, I., Carmel, L., Wolf, Y.I., Mori, H., Savchenko, A.V., Arrowsmith, C.H., Koonin, E.V., Edwards, A.M. and Yakunin, A.F. Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family. J. Biol. Chem. 281 (2006) 36149-36161. [PMID: 16990279]

3. Rawat, R., Sandoval, F.J., Wei, Z., Winkler, R. and Roje, S. An FMN hydrolase of the haloacid dehalogenase superfamily is active in plant chloroplasts. J. Biol. Chem. 286 (2011) 42091-42098. [PMID: 22002057]

[EC 3.1.3.102 created 2016]

EC 3.1.3.103

Accepted name: 3-deoxy-D-glycero-D-galacto-nononate 9-phosphatase

Reaction: 3-deoxy-D-glycero-D-galacto-nononate 9-phosphate + H2O = 3-deoxy-D-glycero-D-galacto-nononate + phosphate

Other name(s): 2-keto-3-deoxy-D-glycero-D-galactonononate-9-phosphate phosphatase

Systematic name: 3-deoxy-D-glycero-D-galacto-nononate 9-phosphohydrolase

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

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Wang, L., Lu, Z., Allen, K.N., Mariano, P.S. and Dunaway-Mariano, D. Human symbiont Bacteroides thetaiotaomicron synthesizes 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN). Chem. Biol. 15 (2008) 893-897. [PMID: 18804026]

2. Lu, Z., Wang, L., Dunaway-Mariano, D. and Allen, K.N. Structure-function analysis of 2-keto-3-deoxy-D-glycero-D-galactonononate-9-phosphate phosphatase defines specificity elements in type C0 haloalkanoate dehalogenase family members. J. Biol. Chem. 284 (2009) 1224-1233. [PMID: 18986982]

[EC 3.1.3.103 created 2016]

EC 3.1.3.104

Accepted name: 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase

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

Other name(s): 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate phosphatase

Systematic name: 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphohydrolase

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

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Haase, I., Sarge, S., Illarionov, B., Laudert, D., Hohmann, H.P., Bacher, A. and Fischer, M. Enzymes from the haloacid dehalogenase (HAD) superfamily catalyse the elusive dephosphorylation step of riboflavin biosynthesis. Chembiochem 14 (2013) 2272-2275. [PMID: 24123841]

2. London, N., Farelli, J.D., Brown, S.D., Liu, C., Huang, H., Korczynska, M., Al-Obaidi, N.F., Babbitt, P.C., Almo, S.C., Allen, K.N. and Shoichet, B.K. Covalent docking predicts substrates for haloalkanoate dehalogenase superfamily phosphatases. Biochemistry 54 (2015) 528-537. [PMID: 25513739]

3. Sarge, S., Haase, I., Illarionov, B., Laudert, D., Hohmann, H.P., Bacher, A. and Fischer, M. Catalysis of an essential step in vitamin B2 biosynthesis by a consortium of broad spectrum hydrolases. ChemBioChem 16 (2015) 2466-2469. [PMID: 26316208]

[EC 3.1.3.104 created 2016]

EC 3.1.3.105

Accepted name: N-acetyl-D-muramate 6-phosphate phosphatase

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

Other name(s): mupP (gene name)

Systematic name: N-acetyl-D-muramate 6-phosphate phosphohydrolase

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

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Borisova, M., Gisin, J. and Mayer, C. The N-acetylmuramic acid 6-phosphate phosphatase MupP completes the Pseudomonas peptidoglycan recycling pathway leading to intrinsic fosfomycin resistance. LID - e00092-17 [pii] LID - 10.1128/mBio.00092-17 [doi. MBio 8 (2017) . [PMID: 28351914]

[EC 3.1.3.105 created 2017]


Continued with EC 3.1.4.1 to EC 3.1.4.51
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