Continued from EC 3.5.4 to EC 3.5.99
EC 3.6.1 In Phosphorus-Containing Anhydrides
EC 3.6.2 In Sulfonyl-Containing Anhydrides
EC 3.6.3 Acting on acid anhydrides; catalysing transmembrane movement of substances
EC 3.6.4 Acting on acid anhydrides; involved in cellular and subcellular movement
EC 3.6.5 Acting on GTP; involved in cellular and subcellular movement
Accepted name: inorganic diphosphatase
Reaction: diphosphate + H2O = 2 phosphate
Systematic name: diphosphate phosphohydrolase
Comments: Specificity varies with the source and with the activating metal ion. The enzyme from some sources may be identical with EC 3.1.3.1 (alkaline phosphatase) or EC 3.1.3.9 (glucose-6-phosphatase). A form of this enzyme with a molecular mass of about 90 kDa is found in tonoplasts of plants and fungi, where it imports protons from the cytosol into the vacuolar lumen.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, PDB, CAS registry number: 9024-82-2
References:
1. Bailey, K. and Webb, E.C. Purification and properties of yeast pyrophosphatase. Biochem. J. 38 (1944) 394-398.
2. Kunitz, M. Crystalline inorganic pyrophosphatase isolated from baker's yeast. J. Gen. Physiol. 35 (1952) 423-450.
3. Rafter, G.W. Pyrophosphate metabolism in liver mitochondria. J. Biol. Chem. 235 (1960) 2475-2477.
Accepted name: trimetaphosphatase
Reaction: trimetaphosphate + H2O = triphosphate
Other name(s): inorganic trimetaphosphatase
Systematic name: trimetaphosphate hydrolase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, CAS registry number: 9024-84-4
References:
1. Kornberg, S.R. Tripolyphosphate and trimetaphosphate in yeast extracts. J. Biol. Chem. 218 (1956) 23-31.
2. Meyerhof, O., Shatas, R. and Kaplan, A. Heat of hydrolysis of trimetaphosphate. Biochim. Biophys. Acta 12 (1953) 121-127.
Accepted name: adenosinetriphosphatase
Reaction: ATP + H2O = ADP + phosphate
Other name(s): adenylpyrophosphatase; ATP monophosphatase; triphosphatase; ATPase; SV40 T-antigen; adenosine 5'-triphosphatase; ATP hydrolase; ATPase; complex V (mitochondrial electron transport); (Ca2+ + Mg2+)-ATPase; HCO3--ATPase; adenosine triphosphatase
Systematic name: ATP phosphohydrolase
Comments: Many enzymes previously listed under this number are now listed separately under EC 3.6.3 and EC 3.6.4.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 9000-83-3
References:
1. Geider, K. and Hofmann-Berling, H. Proteins controlling the helical structure of DNA. Annu. Rev. Biochem. 50 (1981) 233-260. [PMID: 6267987]
2. Kielley, W.W. Myosin adenosine triphosphatase, in Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd edn., vol. 5, Academic Press, New York, 1961, pp. 159-168.
3. Martin, S.S. and Senior, H.E. Membrane adenosine triphosphatase activities in rat pancreas. Biochim. Biophys. Acta 602 (1980) 401-418. [PMID: 6252965]
4. Njus, D., Knoth, J. and Zallakian, M. Proton-linked transport in chromaffin granules. Curr. Top. Bioenerg. 11 (1981) 107-147.
5. Riley, M.V. and Peters, M.I. The localization of the anion-sensitive ATPase activity in corneal endothelium. Biochim. Biophys. Acta 644 (1981) 251-256. [PMID: 6114746]
6. Tjian, R. Regulation of viral transcription and DNA replication by the SV40 large T antigen. Curr. Top. Microbiol. Immunol. 93 (1981) 5-24. [PMID: 6269805]
[EC 3.6.1.4 Deleted entry: adenosinetriphosphatase (Mg-activated). Now included with EC 3.6.1.3 adenosinetriphosphatase (EC 3.6.1.4 created 1961, deleted 1965)]
Accepted name: apyrase
Reaction: ATP + 2 H2O = AMP + 2 phosphate
Other name(s): ATP-diphosphatase; adenosine diphosphatase; ADPase; ATP diphosphohydrolase [ambiguous]
Systematic name: ATP diphosphohydrolase (phosphate-forming)
Comments: Requires Ca2+. Also acts on ADP, and on other nucleoside triphosphates and diphosphates. Most of the ecto-ATPases occurring on the cell surface and hydrolysing extracellular nucleoside triphosphates and diphosphates belong to this enzyme family. Either Ca2+ or Mg2+ can serve as activating ions.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 9000-95-7
References:
1. Krishman, P.S. Apyrase, pyrophosphatase and metaphosphatase of Penicillium chrysogenum. Arch. Biochem. Biophys. 37 (1952) 224-234.
2. Liébecq, C., Lallemand, A. and Degueldre-Guillaume, M.-J. [Partial purification and properties of potato apyrase.] Bull. Soc. Chim. Biol. 45 (1963) 573-594.
Accepted name: nucleoside-diphosphatase
Reaction: A nucleoside diphosphate + H2O = a nucleotide + phosphate
Other name(s): thiaminpyrophosphatase; UDPase; inosine diphosphatase; adenosine diphosphatase; IDPase; ADPase; adenosinepyrophosphatase; guanosine diphosphatase; guanosine 5'-diphosphatase; inosine 5'-diphosphatase; uridine diphosphatase; uridine 5'-diphosphatase; nucleoside diphosphate phosphatase; type B nucleoside diphosphatase; GDPase; CDPase; nucleoside 5'-diphosphatase; type L nucleoside diphosphatase; NDPase; nucleoside diphosphate phosphohydrolase
Systematic name: nucleoside-diphosphate phosphohydrolase
Comments: Acts on IDP, GDP, UDP and also on D-ribose 5-diphosphate
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9027-69-4
References:
1. Gibson, D.M., Ayengar, P. and Sanadi, D.R. A phosphatase specific for nucleoside diphosphates. Biochim. Biophys. Acta 16 (1955) 536-538.
2. Horecker, B.L., Hurwitz, J. and Heppel, L.A. The synthesis of ribose 5-pyrophosphate and ribose 5-triphosphate. J. Am. Chem. Soc. 79 (1957) 701-702.
Accepted name: acylphosphatase
Reaction: An acylphosphate + H2O = a carboxylate + phosphate
Other name(s): acetylphosphatase; 1,3-diphosphoglycerate phosphatase; acetic phosphatase; Ho 1-3; GP 1-3
Systematic name: acylphosphate phosphohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 9012-34-4
References:
1. Raijman, L., Grisolia, S. and Edelhoch, H. Further purification and properties of brain acyl phosphatase.J. Biol. Chem. 235 (1960) 2340-2342.
2. Ramponi, G., Gueritore, A., Treves, C., Nassi, P. and Baccari, V. Horse muscle acyl phosphatase: purification and some properties. Arch. Biochem. Biophys. 130 (1969) 362-369. [PMID: 4305161]
3. Ramponi, G., Nassi, P., Cappugi, G., Treves, C. and Manao, G. Purification and some molecular properties of horse liver acyl phosphatase. Biochim. Biophys. Acta 284 (1972) 485-496. [PMID: 4344156]
4. Shiokawa, H. and Noda, L. Isolation and crystallization of acyl phosphatase from rabbit muscle. J. Biol. Chem. 245 (1970) 669-673. [PMID: 4313603]
Accepted name: ATP diphosphatase
Reaction: ATP + H2O = AMP + diphosphate
Other name(s): ATPase; ATP pyrophosphatase; adenosine triphosphate pyrophosphatase; ATP diphosphohydrolase [ambiguous]
Systematic name: ATP diphosphohydrolase (diphosphate-forming)
Comments: Also acts on ITP, GTP, CTP and UTP.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37289-25-1
References:
1. Heppel, L.A. and Hilmoe, R.J. Mechanism of enzymatic hydrolysis of adenosinetriphosphate. J. Biol. Chem. 202 (1953) 217-226.
2. Johnson, M., Kaye, M.A.G., Hems, R. and Krebs, H.A. Enzymic hydrolysis of adenosine phosphates by cobra venom. Biochem. J. 54 (1953) 625-629.
Accepted name: nucleotide diphosphatase
Reaction: A dinucleotide + H2O = 2 mononucleotides
Other name(s): nucleotide pyrophosphatase; nucleotide-sugar pyrophosphatase
Systematic name: dinucleotide nucleotidohydrolase
Comments: Substrates include NAD+, NADP+, FAD, CoA and also ATP and ADP.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, CAS registry number: 9032-64-8
References:
1. Jacobson, J.B. and Kaplan, N.O. A reduced pyridine nucleotide pyrophosphatase. J. Biol. Chem. 226 (1957) 427-437.
2. Kornberg, A. and Pricer, W.E. Nucleotide pyrophosphatase. J. Biol. Chem. 182 (1950) 763-778.
3. Kumar, S.A., Rao, N.A. and Vaidyanathan, C.S. Nucleotidases in plants. I. Partial purification and properties of the enzyme hydrolyzing flavine adenine dinucleotide from mung bean seedlings (Phaseolus radiatus). Arch. Biochem. Biophys. 111 (1965) 646-652. [PMID: 5862212]
4. Swartz, M.N., Kaplan, N.O. and Lamborg, M.F. A "heat-activated" diphosphopyridine nucleotide pyrophosphatase from Proteus vulgaris. J. Biol. Chem. 232 (1958) 1051-1063.
Accepted name: endopolyphosphatase
Reaction: polyphosphate + n H2O = (n+1) oligophosphate
Other name(s): polyphosphate depolymerase; metaphosphatase; polyphosphatase; polymetaphosphatase
Systematic name: polyphosphate polyphosphohydrolase
Comments: The product contains 4 or 5 phosphate residues.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9024-86-6
References:
1. Malmgren, H. Enzymatic behavior of polymetaphosphate. V. Purification and specificity of the enzyme. Acta Chem. Scand. 6 (1952) 16-26.
2. Mattenheimer, H. Die Substratspezifität "anorganischer" Poly- und Metaphosphatasen. I. Optimale Wirkungsbedingungen für den enzymatischen Abbau von Poly- und Metaphosphaten. Hoppe-Seyler's Z. Physiol. Chem. 303 (1956) 107-114.
Accepted name: exopolyphosphatase
Reaction: (polyphosphate)n + H2O = (polyphosphate)n-1 + phosphate
Other name(s): metaphosphatase; acid phosphoanhydride phosphohydrolase; Gra-Pase
Systematic name: polyphosphate phosphohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9024-85-5
References:
1. Grossman, D. and Lang, K. Anorganische Poly- und Metaphosphatasen sowie Polyphosphate im tierischen Zellkern. Biochem. Z. 336 (1962) 351-370.
2. Krishman, P.S. Apyrase, pyrophosphatase and metaphosphatase of Penicillium chrysogenum. Arch. Biochem. Biophys. 37 (1952) 224-234.
3. Malmgren, H. Enzymatic behavior of polymetaphosphate. V. Purification and specificity of the enzyme. Acta Chem. Scand. 6 (1952) 16-26.
Accepted name: dCTP diphosphatase
Reaction: dCTP + H2O = dCMP + diphosphate
Other name(s): deoxycytidine-triphosphatase; dCTPase; dCTP pyrophosphatase; deoxycytidine triphosphatase; deoxy-CTPase; dCTPase
Systematic name: dCTP nucleotidohydrolase
Comments: Also hydrolyses dCDP to dCMP and phosphate.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9024-87-7
References:
1. Zimmerman, S.B. and Kornberg, A. Deoxycytidine di- and triphosphate cleavage by an enzyme formed in bacteriophage-infected Escherichia coli. J. Biol. Chem. 236 (1961) 1480-1486.
Accepted name: ADP-ribose diphosphatase
Reaction: ADP-ribose + H2O = AMP + D-ribose 5-phosphate
Other name(s): ADPribose pyrophosphatase; adenosine diphosphoribose pyrophosphatase; ADPR-PPase
Systematic name: ADP-ribose ribophosphohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 9024-83-3
References:
1. Doherty, M.D. and Morrison, J.F. The hydrolysis of adenosine diphosphate ribose by a specific phosphohydrolase of rabbit-muscle extracts. Biochim. Biophys. Acta 65 (1962) 364-366.
Accepted name: adenosine-tetraphosphatase
Reaction: adenosine 5'-tetraphosphate + H2O = ATP + phosphate
Systematic name: adenosine-tetraphosphate phosphohydrolase
Comments: Also acts on inosine tetraphosphate and tripolyphosphate but shows little or no activity with other nucleotides or polyphosphates.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37289-26-2
References:
1. Small, G.D. and Cooper, C. Purification and properties of nucleoside tetraphosphate hydrolase from rabbit muscle. Biochemistry 5 (1966) 14-26. [PMID: 4287215]
Accepted name: nucleoside-triphosphatase
Reaction: NTP + H2O = NDP + phosphate
Glossary: thiamine diphosphate
Other name(s): nucleoside triphosphate phosphohydrolase; nucleoside-5-triphosphate phosphohydrolase; nucleoside 5-triphosphatase
Systematic name: unspecific diphosphate phosphohydrolase
Comments: Also hydrolyses other nucleoside triphosphates, diphosphates, thiamine diphosphate and FAD.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 9075-51-8
References:
1. Brightwell, R. and Tappel, A.L. Lysosomal acid pyrophosphatase and acid phosphatase. Arch. Biochem. Biophys. 124 (1968) 333-343. [PMID: 5661608]
2. Lewis, M. and Weissman, S. Properties of a soluble nucleoside triphosphatase activity in mammalian liver. Arch. Biochem. Biophys. 109 (1965) 490-498.
3. Matsushita, S. and Raacke, I.D. Purification of nucleoside triphosphatases from pea seedling ribosomes. Biochim. Biophys. Acta 166 (1968) 707-710. [PMID: 4301913]
Accepted name: CDP-glycerol diphosphatase
Reaction: CDP-glycerol + H2O = CMP + sn-glycerol 3-phosphate
Other name(s): CDP-glycerol pyrophosphatase; cytidine diphosphoglycerol pyrophosphatase
Systematic name: CDP-glycerol phosphoglycerohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37289-28-4
References:
1. Glaser, L. The synthesis of teichoic acid. IV. On the regulation of cytidine 5'-diphosphateglycerol concentration.Biochim. Biophys. Acta 101 (1965) 6-15.
Accepted name: bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)
Reaction: P1,P4-bis(5'-guanosyl) tetraphosphate + H2O = GTP + GMP
Other name(s): bis(5'-guanosyl)-tetraphosphatase; bis(5'-adenosyl)-tetraphosphatase; diguanosinetetraphosphatase (asymmetrical); dinucleosidetetraphosphatase (asymmetrical); diadenosine P1,P4-tetraphosphatase; dinucleoside tetraphosphatase;
Systematic name: P1,P4-bis(5'-nucleosyl)-tetraphosphate nucleotidohydrolase
Comments: Also acts on bis(5'-xanthosyl)-tetraphosphate and, more slowly, on bis(5'-adenosyl)-tetraphosphate and bis(5'-uridyl)-tetraphosphate [cf. EC 3.6.1.41 bis(5'-nucleosyl)-tetraphosphatase (symmetrical)]
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 37289-29-5
References:
1. Jakubowski, H. and Guranowski, A. Enzymes hydrolyzing ApppA and/or AppppA in higher plants. Purification and some properties of diadenosine triphosphatase, diadenosine tetraphosphatase, and phosphodiesterase from yellow lupin (Lupinus luteus) seeds. J. Biol. Chem. 258 (1983) 9982-9989. [PMID: 6309793]
2. Vallejo, C.M., Lobatón, C.D., Quintanilla, M., Sillero, A. and Sillero, M.A.G. Dinucleosidasetetraphosphatase in rat liver and Artemia salina. Biochim. Biophys. Acta 438 (1976) 304-309. [PMID: 181087]
3. Warner, A.H. and Finamore, F.J. Isolation, purification, and characterization of P1,P4-diguanosine 5'-tetraphosphate asymmetrical-pyrophosphohydrolase from brine shrimp eggs. Biochemistry 4 (1965) 1568-1575. [PMID: 4955726]
Accepted name: FAD diphosphatase
Reaction: FAD + H2O = AMP + FMN
Other name(s): FAD pyrophosphatase; riboflavin adenine dinucleotide pyrophosphatase; flavin adenine dinucleotide pyrophosphatase; riboflavine adenine dinucleotide pyrophosphatase; flavine adenine dinucleotide pyrophosphatase
Systematic name: FAD nucleotidohydrolase
Comments: The plant enzyme also hydrolyses NAD+ and NADH; the animal enzyme hydrolyses NAD+ and CoA at about half of the rate of hydrolysis of FAD. May be identical with EC 3.6.1.9 nucleotide diphosphatase.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37289-30-8
References:
1. Ravindranath, S.D. and Appaji Rao, N. Nucleotidases in plants. 3. Effect of metabolites on the enzyme hydrolyzing flavine adenine dinucleotide (FAD) from Phaseolus radiatus. Arch. Biochem. Biophys. 133 (1969) 54-59. [PMID: 5810832]
2. Shin, H.J. and Mego, J.L. A rat liver lysosomal membrane flavin-adenine dinucleotide phosphohydrolase: purification and characterization. Arch. Biochem. Biophys. 267 (1988) 95-103. [PMID: 2848456]
Accepted name: nucleoside-triphosphate diphosphatase
Reaction: A nucleoside triphosphate + H2O = a nucleotide + diphosphate
Other name(s): nucleoside-triphosphate pyrophosphatase
Systematic name: nucleoside-triphosphate diphosphohydrolase
Comments: May be identical with EC 3.6.1.9 nucleotide diphosphatase.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 9075-54-1
References:
1. Chern, C.J., Macdonald, A.B. and Morris, A.J. Purification and properties of a nucleoside triphosphate pyrophosphohydrolase from red cells of the rabbit. J. Biol. Chem. 244 (1969) 5489-5495. [PMID: 4310599]
Accepted name: 5'-acylphosphoadenosine hydrolase
Reaction: 5'-acylphosphoadenosine + H2O = AMP + a carboxylate
Other name(s): 5-phosphoadenosine hydrolase
Systematic name: 5'-acylphosphoadenosine acylhydrolase
Comments: Also acts on inosine and uridine compounds.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37289-31-9
References:
1. Kellerman, G.M. Isolation and characteristics of the enzyme acyl 5'-nucleotidase. Biochim. Biophys. Acta 33 (1959) 101-105.
Accepted name: ADP-sugar diphosphatase
Reaction: ADP-sugar + H2O = AMP + α-D-aldose 1-phosphate
Other name(s): ADP-sugar pyrophosphatase; adenosine diphosphosugar pyrophosphatase
Systematic name: ADP-sugar sugarphosphohydrolase
Comments: Has a specificity that is distinct from that of UDP-sugar diphosphatase (EC 3.6.1.45).
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37289-32-0
References:
1. Rodriguez, P., Bass, S.T. and Hansen, R.G. A pyrophosphatase from mammalian tissues specific for derivatives of ADP. Biochim. Biophys. Acta 167 (1968) 199-201. [PMID: 5686292]
Accepted name: NAD+ diphosphatase
Reaction: NAD+ + H2O = AMP + NMN
Other name(s): nicotinamide adenine dinucleotide pyrophosphatase; NADP pyrophosphatase; NADH pyrophosphatase
Systematic name: NAD+ phosphohydrolase
Comments: Also acts on NADP+, 3-acetylpyridine and the thionicotinamide analogues of NAD+ and NADP+.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37289-33-1
References:
1. Anderson, B.M. and Lang, C.A. Nicotinamide-adenine dinucleotide pyrophosphatase in the growing and aging mosquito. Biochem. J. 101 (1966) 392-396. [PMID: 4381708]
2. Nakajima, Y., Fukunaga, N., Sasaki, S. and Usami, S. Preparation and properties of NADP pyrophosphatase from Proteus vulgaris. Biochim. Biophys. Acta 293 (1973) 242-255.
Accepted name: dUTP diphosphatase
Reaction: dUTP + H2O = dUMP + diphosphate
Other name(s): deoxyuridine-triphosphatase; dUTPase; dUTP pyrophosphatase; desoxyuridine 5'-triphosphate nucleotidohydrolase; desoxyuridine 5'-triphosphatase
Systematic name: dUTP nucleotidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 37289-34-2
References:
1. Bertani, L.E., Häggmark, A. and Reichard, P. Enzymatic synthesis of deoxyribonucleotides. II. Formation and interconversion of deoxyuridine phosphates. J. Biol. Chem. 238 (1963) 3407-3413.
2. Giroir, L.E. and Deutsch, W.A. Drosophila deoxyuridine triphosphatase. Purification and characterization. J. Biol. Chem. 262 (1987) 130-134. [PMID: 3025197]
3. Greenberg, G.R. and Somerville, R.L. Deoxyuridylate kinase activity and deoxyuridinetriphosphatase in Escherichia coli.Proc. Natl. Acad. Sci. USA 48 (1962) 247-257.
4. Grindey, G.B. and Nichol, C.A. Mammalian deoxyuridine 5'-triphosphate pyrophosphatase. Biochim. Biophys. Acta 240 (1971) 180-183. [PMID: 5105331]
Accepted name: nucleoside phosphoacylhydrolase
Reaction: Hydrolyses mixed phospho-anhydride bonds
Systematic name: nucleoside-5'-phosphoacylate acylhydrolase
Comments: Attacks ribonucleoside 5'-nitrophenylphosphates, but is inactive against phosphodiesters.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37289-35-3
References:
1. Spahr, P.F. and Gesteland, R.F. Purification and properties of a new enzyme from Escherichia coli: nucleoside phosphoacyl hydrolase. Eur. J. Biochem. 12 (1970) 270-284. [PMID: 4318904]
Accepted name: triphosphatase
Reaction: triphosphate + H2O = diphosphate + phosphate
Other name(s): inorganic triphosphatase
Systematic name: triphosphate phosphohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 62213-21-2
References:
1. Kulaev, I.S., Konoshenko, G.I. and Umnov, A.M. Localization of polyphosphatase hydolyzing polyphosphates to orthophosphate in subcellular structures of Neurospora crassa. Biochemistry (Moscow) 37 (1972) 190-194.
2. Umnov, A.M., Egorov, S.N., Mansurova, S.E. and Kulaev, I.S. A comparative characterisation of the polyphosphatases of Neurospora crassa and some other organisms. Biochemistry (Moscow) 39 (1974) 309-312.
Accepted name: CDP-diacylglycerol diphosphatase
Reaction: CDP-diacylglycerol + H2O = CMP + phosphatidate
Other name(s): cytidine diphosphodiacylglycerol pyrophosphatase; CDP diacylglycerol hydrolase
Systematic name: CDP-diacylglycerol phosphatidylhydrolase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 62213-20-1
References:
1. Raetz, C.R.H., Hirschberg, B., Dowhan, W., Wickner, W.T. and Kennedy, E.P. A membrane-bound pyrophosphatase in Escherichia coli catalyzing the hydrolysis of cytidine diphosphate-diglyceride. J. Biol. Chem. 247 (1972) 2245-2247. [PMID: 4335869]
Accepted name: undecaprenyl-diphosphatase
Reaction: undecaprenyl diphosphate + H2O = undecaprenyl phosphate + phosphate
For diagram click here.
Other name(s): C55-isoprenyl diphosphatase; C55-isoprenyl pyrophosphatase; isoprenyl pyrophosphatase
Systematic name: undecaprenyl-diphosphate phosphohydrolase
Comments: The undecaprenol involved is ditrans,octacis-undecaprenol (for definitions, click here).
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9077-80-9
References:
1. Goldman, R. and Strominger, J.L. Purification and properties of C55-isoprenylpyrophosphate phosphatase from Micrococcus lysodeikticus. J. Biol. Chem. 247 (1972) 5116-5122. [PMID: 4341539]
Accepted name: thiamine-triphosphatase
Reaction: thiamine triphosphate + H2O = thiamine diphosphate + phosphate
Glossary: thiamine diphosphate
Systematic name: thiamine-triphosphate phosphohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9068-47-7
References:
1. Hashitani, Y. and Cooper, J.R. The partial purification of thiamine triphosphatase from rat brain. J. Biol. Chem. 247 (1972) 2117-2199. [PMID: 4335862]
Accepted name: bis(5'-adenosyl)-triphosphatase
Reaction: P1,P3-bis(5'-adenosyl) triphosphate + H2O = ADP + AMP
Other name(s): dinucleosidetriphosphatase; diadenosine 5,5-P1,P3-triphosphatase
Systematic name: P1,P3-bis(5'-adenosyl)-triphosphate adenylohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 63951-94-0
References:
1. Jakubowski, H. and Guranowski, A. Enzymes hydrolyzing ApppA and/or AppppA in higher plants. Purification and some properties of diadenosine triphosphatase, diadenosine tetraphosphatase, and phosphodiesterase from yellow lupin (Lupinus luteus) seeds. J. Biol. Chem. 258 (1983) 9982-9989. [PMID: 6309793]
2. Sillero, M.A.G., Villalba, R., Morena, A., Quintanilla, M., Lobatón, C.D. and Sillero, A. Dinucleosidetriphosphatase from rat liver. Purification and properties. Eur. J. Biochem. 76 (1977) 331-337. [PMID: 196848]
Accepted name: m7G(5')pppN diphosphatase
Reaction: 7-methylguanosine 5'-triphospho-5'-polynucleotide + H2O = 7-methylguanosine 5'-phosphate + polynucleotide
Other name(s): decapase; m7G(5')pppN pyrophosphatase
Systematic name: 7-methylguanosine-5'-triphospho-5'-polynucleotide 7-methylguanosine-5'-phosphohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 82599-75-5
References:
1. Lavers, G.C. Cleavage of pm7G from mRNA 5' terminal cap structures by pyrophosphatase activity in embryonic chick lens cells. Mol. Biol. Rep. 3 (1977) 413-420. [PMID: 593271]
2. Nuss, D.L., Alschuler, R.E. and Peterson, A.J. Purification and characterization of the m7G(5')pppN-pyrophosphatase from human placenta. J. Biol. Chem. 257 (1982) 6224-6230. [PMID: 6122684]
3. Nuss, D.L. and Furuichi, Y. Characterization of the m7G(5')pppN-pyrophosphatase activity from HeLa cells. J. Biol. Chem. 252 (1977) 2815-2821. [PMID: 16003]
Accepted name: phosphoribosyl-ATP diphosphatase
Reaction: 1-(5-phosphoribosyl)-ATP + H2O = 1-(5-phosphoribosyl)-AMP + diphosphate
For diagram click here.
Other name(s): phosphoribosyl-ATP pyrophosphatase; phosphoribosyladenosine triphosphate pyrophosphatase
Systematic name: 1-(5-phosphoribosyl)-ATP diphosphohydrolase
Comments: The Neurospora crassa enzyme also catalyses the reactions of EC 1.1.1.23 (histidinol dehydrogenase) and EC 3.5.4.19 (phosphoribosyl-AMP cyclohydrolase).
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 69553-55-5
References:
1. Smith, D.W.E. and Ames, B.N. Phosphoribosyladenosine monophosphate, an intermediate in histidine biosynthesis.J. Biol. Chem. 240 (1965) 3056-3063.
[EC 3.6.1.32 transferred entry: now EC 3.6.4.1 myosin ATPase (EC 3.6.1.32 created 1984, deleted 2000)]
[EC 3.6.1.33 transferred entry: now EC 3.6.4.2 dynein ATPase (EC 3.6.1.33 created 1984, deleted 2000)]
[EC 3.6.1.34 transferred entry: now EC 3.6.3.14 H+-transporting two-sector ATPase (EC 3.6.1.34 created 1984, deleted 2000)]
[EC 3.6.1.35 transferred entry: now EC 3.6.3.6 H+-exporting ATPase (EC 3.6.1.35 created 1984, deleted 2000)]
[EC 3.6.1.36 transferred entry: now EC 3.6.3.10 H+/K+-exchanging ATPase (EC 3.6.1.36 created 1984, deleted 2000)]
[EC 3.6.1.37 transferred entry: now EC 3.6.3.9 Na+/K+-exchanging ATPase (EC 3.6.1.37 created 1984, deleted 2000)]
[EC 3.6.1.38 transferred entry: now EC 3.6.3.8 Ca2+-transporting ATPase (EC 3.6.1.38 created 1984, deleted 2000)]
Accepted name: thymidine-triphosphatase
Reaction: dTTP + H2O = dTDP + phosphate
Other name(s): thymidine triphosphate nucleotidohydrolase; dTTPase; deoxythymidine-5'-triphosphatase
Systematic name: dTTP nucleotidohydrolase
Comments: Also acts, more slowly, on dUTP and UTP.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37367-74-1
References:
1. Dahlmann, N. Human serum thymidine triphosphate nucleotidohydrolase: purification and properties of a new enzyme. Biochemistry 21 (1982) 6634-6639. [PMID: 6297538]
Accepted name: guanosine-5'-triphosphate,3'-diphosphate diphosphatase
Reaction: guanosine 5'-triphosphate,3'-diphosphate + H2O = guanosine 5'-diphosphate,3'-diphosphate + phosphate
Other name(s): pppGpp 5'-phosphohydrolase; guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase; guanosine 5'-triphosphate-3'-diphosphate 5'-phosphohydrolase; guanosine pentaphosphatase; guanosine pentaphosphate phosphatase; guanosine 5'-triphosphate 3'-diphosphate 5'-phosphatase; guanosine pentaphosphate phosphohydrolase
Systematic name: guanosine-5'-triphosphate,3'-diphosphate 5'-phosphohydrolase
Comments: Also hydrolyses other guanosine 5'-triphosphate derivatives with at least one unsubstituted phosphate group on the 3'-position, but not GTP, ATP or adenosine 5'-triphosphate,3'-diphosphate.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 85130-44-5
References:
1. Hara, A. and Sy, J. Guanosine 5'-triphosphate, 3'-diphosphate 5'-phosphohydrolase. Purification and substrate specificity. J. Biol. Chem. 258 (1983) 1678-1683. [PMID: 6130093]
Accepted name: bis(5'-nucleosyl)-tetraphosphatase (symmetrical)
Reaction: P1,P4-bis(5'-adenosyl) tetraphosphate + H2O = 2 ADP
Other name(s): diadenosinetetraphosphatase (symmetrical); dinucleosidetetraphosphate (symmetrical); symmetrical diadenosine tetraphosphate hydrolase; adenosine tetraphosphate phosphodiesterase; Ap4A hydrolase; bis(5'-adenosyl) tetraphosphatase; diadenosine tetraphosphate hydrolase; diadenosine polyphosphate hydrolase; diadenosine 5',5'''-P1,P4-tetraphosphatase; diadenosinetetraphosphatase (symmetrical)
Systematic name: P1,P4-bis(5'-nucleosyl)-tetraphosphate nucleosidebisphosphohydrolase
Comments: Also acts on bis(5'-guanosyl) tetraphosphate and bis(5'-adenosyl) pentaphosphate and, more slowly, on some other polyphosphates, forming a nucleoside bisphosphate as one product in all cases [cf. EC 3.6.1.17 bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)].
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 85638-48-8
References:
1. Barnes, L.D. and Culver, C.A. Isolation and characterization of diadenosine 5',5'''-P1,P4-tetraphosphate pyrophosphohydrolase from Physarum polycephalum. Biochemistry 21 (1982) 6123-6128. [PMID: 6295456]
2. Guranowski, A., Jakubowski, H. and Holler, E. Catabolism of diadenosine 5',5'''-P1,P4-tetraphosphate in procaryotes. Purification and properties of diadenosine 5',5'''-P1,P4-tetraphosphate (symmetrical) pyrophosphohydrolase from Escherichia coli K12. J. Biol. Chem. 258 (1983) 14784-14789. [PMID: 6317672]
Accepted name: guanosine-diphosphatase
Reaction: GDP + H2O = GMP + phosphate
Other name(s): GDPase
Systematic name: GDP phosphohydrolase
Comments: Also acts on UDP but not on other nucleoside diphosphates and triphosphates.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 98037-56-0
References:
1. Raychaudhuri, P., Ghosh, S. and Maitra, U. Purification and characterization of a guanosine diphosphatase activity from calf liver microsomal salt wash proteins. J. Biol. Chem. 260 (1985) 8306-8311. [PMID: 2989286]
Accepted name: dolichyldiphosphatase
Reaction: dolichyl diphosphate + H2O = dolichyl phosphate + phosphate
Other name(s): dolichol diphosphatase; dolichyl pyrophosphatase; dolichyl pyrophosphate phosphatase; dolichyl diphosphate phosphohydrolase; Dol-P-P phosphohydrolase
Systematic name: dolichyl-diphosphate phosphohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 73361-26-9
References:
1. Naumov, A.V., Shabalin, Yu.A., Vagabov, V.M. and Kulaev, I.S. Two pathways of dephosphorylation of dolichyl diphosphate in yeasts. Biochemistry (Moscow) 50 (1985) 551-556.
Accepted name: oligosaccharide-diphosphodolichol diphosphatase
Reaction: oligosaccharide-diphosphodolichol + H2O = oligosaccharide phosphate + dolichyl phosphate
Other name(s): oligosaccharide-diphosphodolichol pyrophosphatase
Systematic name: oligosaccharide-diphosphodolichol phosphodolichohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 117698-28-9
References:
1. Belard, M., Cacan, R. and Verbert, A. Characterization of an oligosaccharide-pyrophosphodolichol pyrophosphatase activity in yeast. Biochem. J. 255 (1988) 235-242. [PMID: 2848504]
Accepted name: UDP-sugar diphosphatase
Reaction: UDP-sugar + H2O = UMP + α-D-aldose 1-phosphate
Other name(s): nucleosidediphosphate-sugar pyrophosphatase; nucleosidediphosphate-sugar diphosphatase; UDP-sugar hydrolase; UDP-sugar pyrophosphatase
Systematic name: UDP-sugar sugarphosphohydrolase
Comments: A divalent cation is required for activity. UDP-sugar is the best substrate, although other nucleoside-sugar diphosphates are used as substrates with similar Km values but much lower maximum velocities. Thus, this enzyme has a specificity distinct from that of ADP-sugar diphosphatase (EC 3.6.1.21). Some but not all enzymes of this class also appear to have 5'-nucleotidase (see EC 3.1.3.5) activity.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 55354-38-6
References:
1. Garrett, A.R., Johnson, L.A., Beacham, I.R. Isolation, molecular characterization and expression of the ushB gene of Salmonella typhimurium which encodes a membrane bound UDP-sugar hydrolase. Mol. Microbiol. 3 (1989) 177-186. [PMID: 2548058]
2. Glaser, L., Melo, A., Paul, R. Uridine diphosphate sugar hydrolase. Purification of enzyme and protein inhibitor. J. Biol. Chem. 242 (1987) 1944-1954.
[EC 3.6.1.46 Transferred entry: now EC 3.6.5.1 heterotrimeric G-protein GTPase. (EC 3.6.1.46 created 2000, deleted 2003)]
[TEC 3.6.1.47 ransferred entry: now EC 3.6.5.2 small monomeric GTPase. (EC 3.6.1.47 created 2000, deleted 2003)]
[EC 3.6.1.48 Transferred entry: now EC 3.6.5.3 protein-synthesizing GTPase. (EC 3.6.1.48 created 2000, deleted 200)]
[EC 3.6.1.49 Transferred entry: now EC 3.6.5.4 signal-recognition-particle GTPase. (EC 3.6.1.49 created 2000, deleted 2003)]
[EC 3.6.1.50 Transferred entry: now EC 3.6.5.5 dynamin GTPase. (EC 3.6.1.50 created 2000, deleted 2003)]
[EC 3.6.1.51 Transferred entry: now EC 3.6.5.6 tubulin GTPase. (EC 3.6.1.51 created 2000, deleted 2003)]
Accepted name: diphosphoinositol-polyphosphate diphosphatase
Reaction: diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate
Other name(s): diphosphoinositol-polyphosphate phosphohydrolase; DIPP
Systematic name: diphospho-myo-inositol-polyphosphate diphosphohydrolase
Comments: This enzyme hydrolyses the diphosphate bond, leaving a phospho group where a diphospho group had been. It can also act on bis(adenosine) diphosphate.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Safrany, S.T., Caffrey, J.J., Yang, X., Bembenek, M.E., Moyer, M.B., Burkhart, W.A. and Shears, S.B. A novel context for the 'MutT' module, a guardian of cell integrity, in a diphosphoinositol polyphosphate phosphohydrolase. EMBO J. 17 (1998) 6599-6607. [PMID: 9822604]
2. Caffrey, J.J., Safrany, S.T., Yang, X. and Shears, S.B. Discovery of molecular and catalytic diversity among human diphosphoinositol-polyphosphate phosphohydrolases. An expanding Nudt family. J. Biol. Chem. 275 (2000) 12730-12736. [PMID: 10777568]
Accepted name: Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase
Reaction: (1) CDP-choline + H2O = CMP + phosphocholine
(2) ADP-ribose + H2O = AMP + D-ribose 5-phosphate
Other name(s): Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase; ADPRibase-Mn
Systematic name: CDP-choline phosphohydrolase
Comments: Requires Mn2+, which cannot be replaced by Mg2+, for activity. ADP-ribose, CDP-choline, CDP-ethanolamine and ADP are substrates for this enzyme but ADP-glucose, UDP-glucose, CDP-glucose, CDP, CMP and AMP are not hydrolysed [2]. In rat, the enzyme is found predominantly in thymus and spleen.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Canales, J., Pinto, R.M., Costas, M.J., Hernández, M.T., Miró, A., Bernet, D., Fernández, A. and Cameselle, J.C. Rat liver nucleoside diphosphosugar or diphosphoalcohol pyrophosphatases different from nucleotide pyrophosphatase or phosphodiesterase I: substrate specificities of Mg2+-and/or Mn2+-dependent hydrolases acting on ADP-ribose. Biochim. Biophys. Acta 1246 (1995) 167-177. [PMID: 7819284]
2. Canales, J., Fernández, A., Ribeiro, J.M., Cabezas, A., Rodrigues, J.R., Cameselle, J.C. and Costas, M.J. Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase: a novel metallophosphoesterase family preferentially expressed in rodent immune cells. Biochem. J. 413 (2008) 103-113. [PMID: 18352857]
Accepted name: adenylylsulfatase
Reaction: adenylyl sulfate + H2O = AMP + sulfate
Other name(s): adenosine 5-phosphosulfate sulfohydrolase; adenylylsulfate sulfohydrolase
Systematic name: adenylyl-sulfate sulfohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37289-36-4
References:
1. Bailey-Wood, R., Dodgson, K.S. and Rose, F.A. A rat liver sulphohydrolase enzyme acting on adenylyl sulphate. Biochem. J. 112 (1969) 257-258. [PMID: 5801298]
Accepted name: phosphoadenylylsulfatase
Reaction: 3'-phosphoadenylyl sulfate + H2O = adenosine 3',5'-bisphosphate + sulfate
Other name(s): 3-phosphoadenylyl sulfatase; 3-phosphoadenosine 5-phosphosulfate sulfatase; PAPS sulfatase; 3'-phosphoadenylylsulfate sulfohydrolase
Systematic name: 3'-phosphoadenylyl-sulfate sulfohydrolase
Comments: Requires Mn2+.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37289-37-5
References:
1. Balasubramanian, A.S. and Bachhawat, B.K. Enzymic degradation of active sulphate.Biochim. Biophys. Acta 59 (1962) 389-397.