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). cf. EC 7.1.3.1, H+-exporting diphosphatase.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, 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. [PMID: 16747821]
2. Kunitz, M. Crystalline inorganic pyrophosphatase isolated from baker's yeast. J. Gen. Physiol. 35 (1952) 423-450. [PMID: 14898026]
3. Rafter, G.W. Pyrophosphate metabolism in liver mitochondria. J. Biol. Chem. 235 (1960) 2475-2477. [PMID: 14435825]
Accepted name: trimetaphosphatase
Reaction: trimetaphosphate + H2O = triphosphate
Other name(s): inorganic trimetaphosphatase
Systematic name: trimetaphosphate hydrolase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, 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.
[EC 3.6.1.3 Deleted entry: adenosinetriphosphatase. Enzymes previously listed under this number are now listed separately under EC 5.6 and EC 7. (EC 3.6.1.3 created 1961 (EC 3.6.1.4 created 1961, incorporated 1965), deleted 2020)]
[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: a nucleoside 5'-triphosphate + 2 H2O = a nucleoside 5'-phosphate + 2 phosphate (overall reaction)
(1a) a nucleoside 5'-triphosphate + H2O = a nucleoside 5'-diphosphate + phosphate
(1b) a nucleoside 5'-diphosphate + H2O = a nucleoside 5'-phosphate + phosphate
Other name(s): ATP-diphosphatase (ambiguous); adenosine diphosphatase; ADPase; ATP diphosphohydrolase [ambiguous]
Systematic name: nucleoside triphosphate phosphohydrolase (nucleoside monophosphoate-forming)
Comments: Apyrases are active against both di- and triphosphate nucleotides (NDPs and NTPs) and hydrolyse NTPs to nucleotide monophosphates (NMPs) in two distinct successive phosphate-releasing steps, with NDPs as intermediates. They differ from ATPases, which specifically hydrolyse ATP, by hydrolysing both ATP and ADP. The eukaryotic enzymes requires Ca2+, but Mg2+ can substitute. Most of the ecto-ATPases that occur on the cell surface and hydrolyse extracellular nucleotides belong to this enzyme family.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9000-95-7
References:
1. Krishnan, P.S. Apyrase, pyrophosphatase and metaphosphatase of Penicillium chrysogenum. Arch. Biochem. Biophys. 37 (1952) 224-234. [PMID: 14953432]
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. [PMID: 13930517] (in French)
3. Chen, Y.R., Datta, N. and Roux, S.J. Purification and partial characterization of a calmodulin-stimulated nucleoside triphosphatase from pea nuclei. J. Biol. Chem. 262 (1987) 10689-10694. [PMID: 3038893]
4. Christoforidis, S., Papamarcaki, T., Galaris, D., Kellner, R. and Tsolas, O. Purification and properties of human placental ATP diphosphohydrolase. Eur. J. Biochem. 234 (1995) 66-74. [PMID: 8529670]
5. Wang, T.F. and Guidotti, G. CD39 is an ecto-(Ca2+,Mg2+)-apyrase. J. Biol. Chem. 271 (1996) 9898-9901. [PMID: 8626624]
6. Gao, X.D., Kaigorodov, V. and Jigami, Y. YND1, a homologue of GDA1, encodes membrane-bound apyrase required for Golgi N- and O-glycosylation in Saccharomyces cerevisiae. J. Biol. Chem. 274 (1999) 21450-21456. [PMID: 10409709]
7. Xu, W., Jones, C.R., Dunn, C.A. and Bessman, M.J. Gene ytkD of Bacillus subtilis encodes an atypical nucleoside triphosphatase member of the Nudix hydrolase superfamily. J. Bacteriol. 186 (2004) 8380-8384. [PMID: 15576788]
Accepted name: nucleoside diphosphate phosphatase
Reaction: A nucleoside diphosphate + H2O = a nucleoside phosphate + 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; type B nucleoside diphosphatase; GDPase; CDPase; nucleoside 5'-diphosphatase; type L nucleoside diphosphatase; NDPase; nucleoside diphosphate phosphohydrolase; nucleoside-diphosphatase
Systematic name: nucleoside-diphosphate phosphohydrolase
Comments: The enzyme, which appears to be limited to metazoa, acts on multiple nucleoside diphosphates as well as on D-ribose 5-diphosphate. Specificity depends on species and isoform.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, 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.
3. Yeung, G., Mulero, J.J., McGowan, D.W., Bajwa, S.S. and Ford, J.E. CD39L2, a gene encoding a human nucleoside diphosphatase, predominantly expressed in the heart. Biochemistry 39 (2000) 12916-12923. [PMID: 11041856]
4. Failer, B.U., Braun, N. and Zimmermann, H. Cloning, expression, and functional characterization of a Ca(2+)-dependent endoplasmic reticulum nucleoside diphosphatase. J. Biol. Chem. 277 (2002) 36978-36986. [PMID: 12167635]
5. Uccelletti, D., O'Callaghan, C., Berninsone, P., Zemtseva, I., Abeijon, C. and Hirschberg, C.B. ire-1-dependent transcriptional up-regulation of a lumenal uridine diphosphatase from Caenorhabditis elegans. J. Biol. Chem. 279 (2004) 27390-27398. [PMID: 15102851]
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, Metacyc, 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 (ambiguous); 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, Metacyc, PDB, 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 nucleoside triphosphate + H2O = a nucleotide + diphosphate
Other name(s): ENPP1 (gene name); nucleotide pyrophosphatase; nucleotide-sugar pyrophosphatase; nucleoside-triphosphate diphosphatase
Systematic name: nucleoside-triphosphate diphosphohydrolase
Comments: The enzyme preferentially hydrolyses ATP, but can also hydrolyse other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates. In vitro the enzyme also acts as a nucleotidohydrolase on ADP, NAD+, NADP+, FAD, and CoA.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9032-64-8
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]
2. Kelly, S.J., Dardinger, D.E. and Butler, L.G. Hydrolysis of phosphonate esters catalyzed by 5'-nucleotide phosphodiesterase. Biochemistry 14 (1975) 4983-4988. [PMID: 170964]
3. Landt, M. and Butler, L.G. 5'-Nucleotide phosphodiesterase: isolation of covalently bound 5'-adenosine monophosphate, an intermediate in the catalytic mechanism. Biochemistry 17 (1978) 4130-4135. [PMID: 213103]
4. Zhang, J. and Inouye, M. MazG, a nucleoside triphosphate pyrophosphohydrolase, interacts with Era, an essential GTPase in Escherichia coli. J. Bacteriol. 184 (2002) 5323-5329. [PMID: 12218018]
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, Metacyc, 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, Metacyc, PDB, 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): DCTPP1 (gene name); deoxycytidine-triphosphatase; dCTPase; dCTP pyrophosphatase; deoxycytidine triphosphatase; deoxy-CTPase
Systematic name: dCTP nucleotidohydrolase
Comments: The mammalian enzyme also displays weak activity against dTTP and dATP, but none against dGTP. Activity is highest with analogs including 5-iodo-dCTP and 5-methyl-dCTP.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, 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.
2. Moroz, O.V., Murzin, A.G., Makarova, K.S., Koonin, E.V., Wilson, K.S. and Galperin, M.Y. Dimeric dUTPases, HisE, and MazG belong to a new superfamily of all-α NTP pyrophosphohydrolases with potential "house-cleaning" functions. J. Mol. Biol. 347 (2005) 243-255. [PMID: 15740738]
3. Wu, B., Liu, Y., Zhao, Q., Liao, S., Zhang, J., Bartlam, M., Chen, W. and Rao, Z. Crystal structure of RS21-C6, involved in nucleoside triphosphate pyrophosphohydrolysis. J. Mol. Biol. 367 (2007) 1405-1412. [PMID: 17320107]
4. Nonaka, M., Tsuchimoto, D., Sakumi, K. and Nakabeppu, Y. Mouse RS21-C6 is a mammalian 2'-deoxycytidine 5'-triphosphate pyrophosphohydrolase that prefers 5-iodocytosine. FEBS J. 276 (2009) 1654-1666. [PMID: 19220460]
5. Requena, C.E., Perez-Moreno, G., Ruiz-Perez, L.M., Vidal, A.E. and Gonzalez-Pacanowska, D. The NTP pyrophosphatase DCTPP1 contributes to the homoeostasis and cleansing of the dNTP pool in human cells. Biochem. J. 459 (2014) 171-180. [PMID: 24467396]
Accepted name: ADP-ribose diphosphatase
Reaction: ADP-α-D-ribose + H2O = AMP + D-ribose 5-phosphate
Other name(s): ADPribose pyrophosphatase; adenosine diphosphoribose pyrophosphatase; ADPR-PPase; ADP-ribose ribophosphohydrolase
Systematic name: ADP-α-D-ribose ribophosphohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, 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, Metacyc, PDB, 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-triphosphate phosphatase
Reaction: a nucleoside triphosphate + H2O = a nucleoside diphosphate + phosphate
Other name(s): nucleoside triphosphate phosphohydrolase; nucleoside-5-triphosphate phosphohydrolase; nucleoside 5-triphosphatase; nucleoside-triphosphatase; unspecific diphosphate phosphohydrolase
Systematic name: nucleoside-triphosphate phosphohydrolase
Comments: The enzyme is found in eukaryotes and thermophilic bacteria, but appears to be absent from mesophilic bacteria. Also hydrolyses nucleoside diphosphates, thiamine diphosphate and FAD. The enzyme from the plant Pisum sativum (garden pea) is regulated by calmodulin [5].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, 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]
4. Tong, C.G., Dauwalder, M., Clawson, G.A., Hatem, C.L. and Roux, S.J. The major nucleoside triphosphatase in pea (Pisum sativum L.) nuclei and in rat liver nuclei share common epitopes also present in nuclear lamins. Plant Physiol. 101 (1993) 1005-1011. [PMID: 7508630]
5. Hsieh, H.L., Tong, C.G., Thomas, C. and Roux, S.J. Light-modulated abundance of an mRNA encoding a calmodulin-regulated, chromatin-associated NTPase in pea. Plant Mol. Biol. 30 (1996) 135-147. [PMID: 8616230]
6. Klinger, C., Rossbach, M., Howe, R. and Kaufmann, M. Thermophile-specific proteins: the gene product of aq_1292 from Aquifex aeolicus is an NTPase. BMC Biochem. 4 (2003) 12. [PMID: 14503925]
7. Placzek, W.J., Almeida, M.S. and Wuthrich, K. NMR structure and functional characterization of a human cancer-related nucleoside triphosphatase. J. Mol. Biol. 367 (2007) 788-801. [PMID: 17291528]
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, Metacyc, PDB, 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, Metacyc, 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
For diagram of reaction click here.
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, Metacyc, 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]
[EC 3.6.1.19 Transferred entry: nucleoside-triphosphate diphosphatase, now included in EC 3.6.1.9, nucleotide diphosphatase (EC 3.6.1.19 created 1972, deleted 2016)]
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, Metacyc, 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, Metacyc, 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, Metacyc, PDB, CAS registry number: 37289-33-1
References:
1. Kornberg, A. and Pricer, W.E. Nucleotide pyrophosphatase. J. Biol. Chem. 182 (1950) 763-778.
2. Jacobson, J.B. and Kaplan, N.O. A reduced pyridine nucleotide pyrophosphatase. J. Biol. Chem. 226 (1957) 427-437. [PMID: 13428775]
3. 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. [PMID: 13549486]
4. 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]
5. 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]
6. 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. [PMID: 4405504]
7. Frick, D.N. and Bessman, M.J. Cloning, purification, and properties of a novel NADH pyrophosphatase. Evidence for a nucleotide pyrophosphatase catalytic domain in MutT-like enzymes. J. Biol. Chem. 270 (1995) 1529-1534. [PMID: 7829480]
8. Xu, W., Dunn, C.A. and Bessman, M.J. Cloning and characterization of the NADH pyrophosphatases from Caenorhabditis elegans and Saccharomyces cerevisiae, members of a Nudix hydrolase subfamily. Biochem. Biophys. Res. Commun. 273 (2000) 753-758. [PMID: 10873676]
9. Jambunathan, N. and Mahalingam, R. Analysis of Arabidopsis growth factor gene 1 (GFG1) encoding a nudix hydrolase during oxidative signaling. Planta 224 (2006) 1-11. [PMID: 16328543]
Accepted name: dUTP diphosphatase
Reaction: dUTP + H2O = dUMP + diphosphate
Other name(s): DUT (gene name); deoxyuridine-triphosphatase; dUTPase; dUTP pyrophosphatase; desoxyuridine 5'-triphosphate nucleotidohydrolase; desoxyuridine 5'-triphosphatase
Systematic name: dUTP nucleotidohydrolase
Comments: The enzyme catalyses the Mg2+-dependent hydrolysis of dUTP to dUMP, providing the substrate for EC 2.1.1.45, thymidylate synthase, leading to production of thymidine nucleotides. By reducing the effective ratio of dUTP to TTP, the enzyme also reduces the possibility of dUTP incorporation into DNA.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37289-34-2
References:
1. Greenberg, G.R. and Somerville, R.L. Deoxyuridylate kinase activity and deoxyuridinetriphosphatase in Escherichia coli. Proc. Natl. Acad. Sci. USA 48 (1962) 247-257. [PMID: 13901467]
2. 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. [PMID: 14085395]
3. Grindey, G.B. and Nichol, C.A. Mammalian deoxyuridine 5'-triphosphate pyrophosphatase. Biochim. Biophys. Acta 240 (1971) 180-183. [PMID: 5105331]
4. Shlomai, J. and Kornberg, A. Deoxyuridine triphosphatase of Escherichia coli. Purification, properties, and use as a reagent to reduce uracil incorporation into DNA. J. Biol. Chem. 253 (1978) 3305-3312. [PMID: 346589]
5. Giroir, L.E. and Deutsch, W.A. Drosophila deoxyuridine triphosphatase. Purification and characterization. J. Biol. Chem. 262 (1987) 130-134. [PMID: 3025197]
6. Cedergren-Zeppezauer, E.S., Larsson, G., Nyman, P.O., Dauter, Z. and Wilson, K.S. Crystal structure of a dUTPase. Nature 355 (1992) 740-743. [PMID: 1311056]
7. Ladner, R.D., McNulty, D.E., Carr, S.A., Roberts, G.D. and Caradonna, S.J. Characterization of distinct nuclear and mitochondrial forms of human deoxyuridine triphosphate nucleotidohydrolase. J. Biol. Chem. 271 (1996) 7745-7751. [PMID: 8631816]
8. Bajaj, M. and Moriyama, H. Purification, crystallization and preliminary crystallographic analysis of deoxyuridine triphosphate nucleotidohydrolase from Arabidopsis thaliana. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63 (2007) 409-411. [PMID: 17565183]
9. Varga, B., Barabas, O., Kovari, J., Toth, J., Hunyadi-Gulyas, E., Klement, E., Medzihradszky, K.F., Tolgyesi, F., Fidy, J. and Vertessy, B.G. Active site closure facilitates juxtaposition of reactant atoms for initiation of catalysis by human dUTPase. FEBS Lett. 581 (2007) 4783-4788. [PMID: 17880943]
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, Metacyc, 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, Metacyc, PDB, 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, Metacyc, PDB, 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-diphosphate phosphatase
Reaction: ditrans,octacis-undecaprenyl diphosphate + H2O = ditrans,octacis-undecaprenyl phosphate + phosphate
For diagram of reaction click here or click here.
Other name(s): C55-isoprenyl diphosphatase; C55-isoprenyl pyrophosphatase; isoprenyl pyrophosphatase (ambiguous); undecaprenyl pyrophosphate phosphatase; undecaprenyl pyrophosphate pyrophosphatase; UPP phosphatase; Und-PP pyrophosphatase; UppP (ambiguous); BacA; undecaprenyl-diphosphate phosphohydrolase; undecaprenyl-diphosphatase
Systematic name: ditrans,octacis-undecaprenyl-diphosphate phosphohydrolase
Comments: Isolated from the bacteria Micrococcus lysodeikticus [1], Escherichia coli [2,3,5,6] and Bacillus subtilis [4]. The product of the reaction, ditrans,octacis-undecaprenyl phosphate, is essential for cell wall polysaccharide biosynthesis in these strains.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, 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]
2. El Ghachi, M., Bouhss, A., Blanot, D. and Mengin-Lecreulx, D. The bacA gene of Escherichia coli encodes an undecaprenyl pyrophosphate phosphatase activity. J. Biol. Chem. 279 (2004) 30106-30113. [PMID: 15138271]
3. El Ghachi, M., Derbise, A., Bouhss, A. and Mengin-Lecreulx, D. Identification of multiple genes encoding membrane proteins with undecaprenyl pyrophosphate phosphatase (UppP) activity in Escherichia coli. J. Biol. Chem. 280 (2005) 18689-18695. [PMID: 15778224]
4. Bernard, R., El Ghachi, M., Mengin-Lecreulx, D., Chippaux, M. and Denizot, F. BcrC from Bacillus subtilis acts as an undecaprenyl pyrophosphate phosphatase in bacitracin resistance. J. Biol. Chem. 280 (2005) 28852-28857. [PMID: 15946938]
5. Tatar, L.D., Marolda, C.L., Polischuk, A.N., van Leeuwen, D. and Valvano, M.A. An Escherichia coli undecaprenyl-pyrophosphate phosphatase implicated in undecaprenyl phosphate recycling. Microbiology 153 (2007) 2518-2529. [PMID: 17660416]
6. Touze, T., Blanot, D. and Mengin-Lecreulx, D. Substrate specificity and membrane topology of Escherichia coli PgpB, an undecaprenyl pyrophosphate phosphatase. J. Biol. Chem. 283 (2008) 16573-16583. [PMID: 18411271]
Accepted name: thiamine-triphosphatase
Reaction: thiamine triphosphate + H2O = thiamine diphosphate + phosphate
For diagram of reaction click here.
Glossary: thiamine diphosphate
Systematic name: thiamine-triphosphate phosphohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, 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, Metacyc, 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]
[EC 3.6.1.30 Deleted entry: m7G(5')pppN diphosphatase. Now covered by EC 3.6.1.59 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase and EC 3.6.1.62 [m7GpppN-mRNA hydrolase]. (EC 3.6.1.30 created 1978, deleted 2012)]
Accepted name: phosphoribosyl-ATP diphosphatase
Reaction: 1-(5-phospho-β-D-ribosyl)-ATP + H2O = 1-(5-phospho-β-D-ribosyl)-AMP + diphosphate
For diagram click here.
Other name(s): phosphoribosyl-ATP pyrophosphatase; phosphoribosyladenosine triphosphate pyrophosphatase; 1-(5-phosphoribosyl)-ATP diphosphohydrolase
Systematic name: 1-(5-phospho-β-D-ribosyl)-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, Metacyc, PDB, 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, Metacyc, 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 phosphatase
Reaction: guanosine 5'-triphosphate 3'-diphosphate + H2O = guanosine 3',5'-bis(diphosphate) + phosphate
Other name(s): pppGpp 5'-phosphohydrolase; 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, Metacyc, PDB, 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, Metacyc, PDB, 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, Metacyc, PDB, 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, Metacyc, 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, Metacyc, 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, Metacyc, 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, Metacyc, PDB, 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-D-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+. Unlike EC 3.6.1.13, ADP-ribose diphosphatase, it cannot utilize Mg2+. ADP-D-ribose, CDP-choline, CDP-ethanolamine and ADP are substrates for this enzyme but ADP-D-glucose, UDP-D-glucose, CDP-D-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, Metacyc, PDB, 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]
3. Canales, J., Fernandez, A., Rodrigues, J.R., Ferreira, R., Ribeiro, J.M., Cabezas, A., Costas, M.J. and Cameselle, J.C. Hydrolysis of the phosphoanhydride linkage of cyclic ADP-ribose by the Mn(2+)-dependent ADP-ribose/CDP-alcohol pyrophosphatase. FEBS Lett 583 (2009) 1593-1598. [PMID: 19379742]
4. Rodrigues, J.R., Fernandez, A., Canales, J., Cabezas, A., Ribeiro, J.M., Costas, M.J. and Cameselle, J.C. Characterization of Danio rerio Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase, the structural prototype of the ADPRibase-Mn-like protein family. PLoS One 7 (2012) e42249. [PMID: 22848751]
Accepted name: UDP-2,3-diacylglucosamine diphosphatase
Reaction: a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine + H2O = a lipid X + UMP
For diagram of reaction click here
Glossary: a lipid X = 2-N-[(3R)-3-hydroxyacyl]-3-O-[(3R)-3-hydroxyacyl]-α-D-glucosamine 1-phosphate =
2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine
Other name(s): lpxH (gene name); UDP-2,3-diacylglucosamine hydrolase; UDP-2,3-diacylglucosamine pyrophosphatase; ybbF (gene name); UDP-2,3-bis[(3R)-3-hydroxymyristoyl]-α-D-glucosamine 2,3-bis[(3R)-3-hydroxymyristoyl]-β-D-glucosaminyl 1-phosphate phosphohydrolase (incorrect); UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-α-D-glucosamine 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-α-D-glucosaminyl 1-phosphate phosphohydrolase
Systematic name: UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine 2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine-1-phosphate phosphohydrolase
Comments: The enzyme catalyses a step in the biosynthesis of lipid A.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Babinski, K.J., Ribeiro, A.A. and Raetz, C.R. The Escherichia coli gene encoding the UDP-2,3-diacylglucosamine pyrophosphatase of lipid A biosynthesis. J. Biol. Chem. 277 (2002) 25937-25946. [PMID: 12000770]
2. Babinski, K.J., Kanjilal, S.J. and Raetz, C.R. Accumulation of the lipid A precursor UDP-2,3-diacylglucosamine in an Escherichia coli mutant lacking the lpxH gene. J. Biol. Chem. 277 (2002) 25947-25956. [PMID: 12000771]
3. Okada, C., Wakabayashi, H., Kobayashi, M., Shinoda, A., Tanaka, I. and Yao, M. Crystal structures of the UDP-diacylglucosamine pyrophosphohydrase LpxH from Pseudomonas aeruginosa, Sci. Rep. 6 (2016) 32822. [PMID: 27609419]
4. Cho, J., Lee, C.J., Zhao, J., Young, H.E. and Zhou, P. Structure of the essential Haemophilus influenzae UDP-diacylglucosamine pyrophosphohydrolase LpxH in lipid A biosynthesis. Nat Microbiol 1 (2016) 16154. [PMID: 27780190]
5. Arenas, J., Pupo, E., de Jonge, E., Perez-Ortega, J., Schaarschmidt, J., van der Ley, P. and Tommassen, J. Substrate specificity of the pyrophosphohydrolase LpxH determines the asymmetry of Bordetella pertussis lipid A. J. Biol. Chem. 294 (2019) 7982-7989. [PMID: 30926608]
Accepted name: 8-oxo-dGTP diphosphatase
Reaction: 8-oxo-dGTP + H2O = 8-oxo-dGMP + diphosphate
Glossary: 8-oxo-dGTP = 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate
Other name(s): MutT; 7,8-dihydro-8-oxoguanine triphosphatase; 8-oxo-dGTPase; 7,8-dihydro-8-oxo-dGTP pyrophosphohydrolase
Systematic name: 8-oxo-dGTP diphosphohydrolase
Comments: This enzyme hydrolyses the phosphoanhydride bond between the α and β phosphate of 8-oxoguanine-containing nucleoside di- and triphosphates thereby preventing misincorporation of the oxidized purine nucleoside triphosphates into DNA . It does not hydrolyse 2-hydroxy-dATP (cf. EC 3.6.1.56, 2-hydroxy-dATP diphosphatase) [4]. Requires Mg2+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Ito, R., Hayakawa, H., Sekiguchi, M. and Ishibashi, T. Multiple enzyme activities of Escherichia coli MutT protein for sanitization of DNA and RNA precursor pools. Biochemistry 44 (2005) 6670-6674. [PMID: 15850400]
2. Yoshimura, K., Ogawa, T., Ueda, Y. and Shigeoka, S. AtNUDX1, an 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate pyrophosphohydrolase, is responsible for eliminating oxidized nucleotides in Arabidopsis. Plant Cell Physiol. 48 (2007) 1438-1449. [PMID: 17804481]
3. Nakamura, T., Meshitsuka, S., Kitagawa, S., Abe, N., Yamada, J., Ishino, T., Nakano, H., Tsuzuki, T., Doi, T., Kobayashi, Y., Fujii, S., Sekiguchi, M. and Yamagata, Y. Structural and dynamic features of the MutT protein in the recognition of nucleotides with the mutagenic 8-oxoguanine base. J. Biol. Chem. 285 (2010) 444-452. [PMID: 19864691]
4. Yonekura, S., Sanada, U. and Zhang-Akiyama, Q.M. CiMutT, an asidian MutT homologue, has a 7, 8-dihydro-8-oxo-dGTP pyrophosphohydrolase activity responsible for sanitization of oxidized nucleotides in Ciona intestinalis. Genes Genet Syst 85 (2010) 287-295. [PMID: 21178309]
Accepted name: 2-hydroxy-dATP diphosphatase
Reaction: 2-hydroxy-dATP + H2O = 2-hydroxy-dAMP + diphosphate
Other name(s): NUDT1; MTH1; MTH2; oxidized purine nucleoside triphosphatase; (2'-deoxy) ribonucleoside 5'-triphosphate pyrophosphohydrolase
Systematic name: 2-hydroxy-dATP diphosphohydrolase
Comments: The enzyme hydrolyses oxidized purine nucleoside triphosphates such as 2-hydroxy-dATP, thereby preventing their misincorporation into DNA. It can also recognize 8-oxo-dGTP and 8-oxo-dATP, but with lower efficiency (cf. EC 3.6.1.55, 8-oxo-dGTP diphosphatase) [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Sakumi, K., Furuichi, M., Tsuzuki, T., Kakuma, T., Kawabata, S., Maki, H. and Sekiguchi, M. Cloning and expression of cDNA for a human enzyme that hydrolyzes 8-oxo-dGTP, a mutagenic substrate for DNA synthesis. J. Biol. Chem. 268 (1993) 23524-23530. [PMID: 8226881]
2. Kakuma, T., Nishida, J., Tsuzuki, T. and Sekiguchi, M. Mouse MTH1 protein with 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphatase activity that prevents transversion mutation. cDNA cloning and tissue distribution. J. Biol. Chem. 270 (1995) 25942-25948. [PMID: 7592783]
3. Fujikawa, K., Kamiya, H., Yakushiji, H., Fujii, Y., Nakabeppu, Y. and Kasai, H. The oxidized forms of dATP are substrates for the human MutT homologue, the hMTH1 protein. J. Biol. Chem. 274 (1999) 18201-18205. [PMID: 10373420]
4. Sakai, Y., Furuichi, M., Takahashi, M., Mishima, M., Iwai, S., Shirakawa, M. and Nakabeppu, Y. A molecular basis for the selective recognition of 2-hydroxy-dATP and 8-oxo-dGTP by human MTH1. J. Biol. Chem. 277 (2002) 8579-8587. [PMID: 11756418]
5. Fujikawa, K., Kamiya, H., Yakushiji, H., Nakabeppu, Y. and Kasai, H. Human MTH1 protein hydrolyzes the oxidized ribonucleotide, 2-hydroxy-ATP. Nucleic Acids Res. 29 (2001) 449-454. [PMID: 11139615]
Accepted name: UDP-2,4-diacetamido-2,4,6-trideoxy-β-L-altropyranose hydrolase
Reaction: UDP-2,4-diacetamido-2,4,6-trideoxy-β-L-altropyranose + H2O = 2,4-diacetamido-2,4,6-trideoxy-β-L-altropyranose + UDP
Glossary: pseudaminic acid = 5,7-diacetamido-3,5,7,9-tetradeoxy-L-glycero-α-L-manno-2-nonulopyranosonic acid
Other name(s): PseG; UDP-6-deoxy-AltdiNAc hydrolase; Cj1312; UDP-2,4-bis(acetamido)-2,4,6-trideoxy-β-L-altropyranose hydrolase
Systematic name: UDP-2,4-diacetamido-2,4,6-trideoxy-β-L-altropyranose hydrolase
Comments: The enzyme is involved in biosynthesis of pseudaminic acid.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Liu, F. and Tanner, M.E. PseG of pseudaminic acid biosynthesis: a UDP-sugar hydrolase as a masked glycosyltransferase. J. Biol. Chem. 281 (2006) 20902-20909. [PMID: 16728396]
2. Schoenhofen, I.C., McNally, D.J., Brisson, J.R. and Logan, S.M. Elucidation of the CMP-pseudaminic acid pathway in Helicobacter pylori: synthesis from UDP-N-acetylglucosamine by a single enzymatic reaction. Glycobiology 16 (2006) 8C. [PMID: 16751642]
Accepted name: 8-oxo-dGDP phosphatase
Reaction: (1) 8-oxo-dGDP + H2O = 8-oxo-dGMP + phosphate
(2) 8-oxo-GDP + H2O = 8-oxo-GMP + phosphate
Glossary: 8-oxo-dGDP = 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-diphosphate
Other name(s): NUDT5; MTH3 (gene name); NUDT18
Systematic name: 8-oxo-dGDP phosphohydrolase
Comments: The enzyme catalyses the hydrolysis of both 8-oxo-dGDP and 8-oxo-GDP thereby preventing translational errors caused by oxidative damage. The preferred in vivo substrate is not known. The enzyme does not degrade 8-oxo-dGTP and 8-oxo-GTP to the monophosphates (cf. EC 3.6.1.55, 8-oxo-dGTP diphosphatase) [1,2]. Ribonucleotide diphosphates and deoxyribonucleotide diphosphates are hydrolysed with broad specificity. The bifunctional enzyme NUDT5 also hydrolyses ADP-ribose to AMP and D-ribose 5-phosphate (cf. EC 3.6.1.13, ADP-ribose diphosphatase) [4]. The human enzyme NUDT18 also hydrolyses 8-oxo-dADP and 2-hydroxy-dADP, the latter at a slower rate [6].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Ishibashi, T., Hayakawa, H., Ito, R., Miyazawa, M., Yamagata, Y. and Sekiguchi, M. Mammalian enzymes for preventing transcriptional errors caused by oxidative damage. Nucleic Acids Res. 33 (2005) 3779-3784. [PMID: 16002790]
2. Ishibashi, T., Hayakawa, H. and Sekiguchi, M. A novel mechanism for preventing mutations caused by oxidation of guanine nucleotides. EMBO Rep. 4 (2003) 479-483. [PMID: 12717453]
3. Kamiya, H., Hori, M., Arimori, T., Sekiguchi, M., Yamagata, Y. and Harashima, H. NUDT5 hydrolyzes oxidized deoxyribonucleoside diphosphates with broad substrate specificity. DNA Repair (Amst) 8 (2009) 1250-1254. [PMID: 19699693]
4. Ito, R., Sekiguchi, M., Setoyama, D., Nakatsu, Y., Yamagata, Y. and Hayakawa, H. Cleavage of oxidized guanine nucleotide and ADP sugar by human NUDT5 protein. J. Biochem. 149 (2011) 731-738. [PMID: 21389046]
5. Zha, M., Zhong, C., Peng, Y., Hu, H. and Ding, J. Crystal structures of human NUDT5 reveal insights into the structural basis of the substrate specificity. J. Mol. Biol. 364 (2006) 1021-1033. [PMID: 17052728]
6. Takagi, Y., Setoyama, D., Ito, R., Kamiya, H., Yamagata, Y. and Sekiguchi, M. Human MTH3 (NUDT18) protein hydrolyzes oxidized forms of guanosine and deoxyguanosine diphosphates: comparison with MTH1 and MTH2. J. Biol. Chem. 287 (2012) 21541-21549. [PMID: 22556419]
Accepted name: 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase
Reaction: a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] + H2O = N7-methylguanosine 5'-phosphate + a 5'-diphospho-[mRNA]
Other name(s): DcpS; m7GpppX pyrophosphatase; m7GpppN m7GMP phosphohydrolase; m7GpppX diphosphatase; m7G5'ppp5’N m7GMP phosphohydrolase
Systematic name: 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] N7-methylguanosine 5'-phosphate phosphohydrolase
Comments: The enzyme removes (decaps) the N7-methylguanosine 5-phosphate cap from an mRNA degraded to a maximal length of 10 nucleotides [3,6]. Decapping is an important process in the control of eukaryotic mRNA degradation. The enzyme functions to clear the cell of cap structure following decay of the RNA body [2]. The nematode enzyme can also decap triply methylated substrates, 5'-(N2,N2,N7-trimethyl 5'-triphosphoguanosine)-[mRNA] [4].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Malys, N. and McCarthy, J.E. Dcs2, a novel stress-induced modulator of m7GpppX pyrophosphatase activity that locates to P bodies. J. Mol. Biol. 363 (2006) 370-382. [PMID: 16963086]
2. Liu, S.W., Rajagopal, V., Patel, S.S. and Kiledjian, M. Mechanistic and kinetic analysis of the DcpS scavenger decapping enzyme. J. Biol. Chem. 283 (2008) 16427-16436. [PMID: 18441014]
3. Liu, H., Rodgers, N.D., Jiao, X. and Kiledjian, M. The scavenger mRNA decapping enzyme DcpS is a member of the HIT family of pyrophosphatases. EMBO J. 21 (2002) 4699-4708. [PMID: 12198172]
4. van Dijk, E., Le Hir, H. and Seraphin, B. DcpS can act in the 5'-3' mRNA decay pathway in addition to the 3'-5' pathway. Proc. Natl. Acad. Sci. USA 100 (2003) 12081-12086. [PMID: 14523240]
5. Chen, N., Walsh, M.A., Liu, Y., Parker, R. and Song, H. Crystal structures of human DcpS in ligand-free and m7GDP-bound forms suggest a dynamic mechanism for scavenger mRNA decapping. J. Mol. Biol. 347 (2005) 707-718. [PMID: 15769464]
6. Cohen, L.S., Mikhli, C., Friedman, C., Jankowska-Anyszka, M., Stepinski, J., Darzynkiewicz, E. and Davis, R.E. Nematode m7GpppG and m3(2,2,7)GpppG decapping: activities in Ascaris embryos and characterization of C. elegans scavenger DcpS. RNA 10 (2004) 1609-1624. [PMID: 15383679]
7. Wypijewska, A., Bojarska, E., Lukaszewicz, M., Stepinski, J., Jemielity, J., Davis, R.E. and Darzynkiewicz, E. 7-Methylguanosine diphosphate (m7GDP) is not hydrolyzed but strongly bound by decapping scavenger (DcpS) enzymes and potently inhibits their activity. Biochemistry 51 (2012) 8003-8013. [PMID: 22985415]
Accepted name: diadenosine hexaphosphate hydrolase (AMP-forming)
Reaction: (1) P1,P6-bis(5'-adenosyl)hexaphosphate + H2O = adenosine 5'-pentaphosphate + AMP
(2) P1,P5-bis(5'-adenosyl)pentaphosphate + H2O = adenosine 5'-tetraphosphate + AMP
Other name(s): hAps1; NUDT11 (gene name); hAps2; NUDT10 (gene name)
Systematic name: P1,P6-bis(5'-adenosyl)hexaphosphate nucleotidohydrolase (AMP-forming)
Comments: A divalent cation is essential for activity. Mn2+ (2-6 mM) is most effective. The enzyme controls intracellular levels of P1,P5-bis(5'-adenosyl)pentaphosphate and P1,P6-bis(5'-adenosyl)hexaphosphate. Weak activity with P1,P4-bis(5'-adenosyl)tetraphosphate. Marked preference for adenine over guanine nucleotides.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Leslie, N.R., McLennan, A.G. and Safrany, S.T. Cloning and characterisation of hAps1 and hAps2, human diadenosine polyphosphate-metabolising Nudix hydrolases. BMC Biochem 3 (2002) 20. [PMID: 12121577]
2. Safrany, S.T., Ingram, S.W., Cartwright, J.L., Falck, J.R., McLennan, A.G., Barnes, L.D. and Shears, S.B. The diadenosine hexaphosphate hydrolases from Schizosaccharomyces pombe and Saccharomyces cerevisiae are homologues of the human diphosphoinositol polyphosphate phosphohydrolase. Overlapping substrate specificities in a MutT-type protein. J. Biol. Chem. 274 (1999) 21735-21740. [PMID: 10419486]
Accepted name: diadenosine hexaphosphate hydrolase (ATP-forming)
Reaction: (1) P1,P6-bis(5'-adenosyl)hexaphosphate + H2O = 2 ATP
(2) P1,P5-bis(5'-adenosyl)pentaphosphate + H2O = ATP + ADP
(3) P1,P4-bis(5'-adenosyl)tetraphosphate + H2O = ATP + AMP
Other name(s): Ndx1
Systematic name: P1,P6-bis(5'-adenosyl)hexaphosphate nucleotidohydrolase (ATP-forming)
Comments: The enzyme requires the presence of the divalent cations (Mn2+, Mg2+, Zn2+, and Co2+). It hydrolyses P1,P4-bis(5-guanosyl) tetraphosphate very slowly [cf. EC 3.6.1.17, bis(5-nucleosyl)-tetraphosphatase (asymmetrical)].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Iwai, T., Kuramitsu, S. and Masui, R. The Nudix hydrolase Ndx1 from Thermus thermophilus HB8 is a diadenosine hexaphosphate hydrolase with a novel activity. J. Biol. Chem. 279 (2004) 21732-21739. [PMID: 15024014]
Accepted name: 5'-(N7-methylguanosine 5'-triphospho)-[mRNA] hydrolase
Reaction: a 5'-(N7-methylguanosine 5'-triphospho)-[mRNA] + H2O = N7-methylguanosine 5'-diphosphate + a 5'-phospho-[mRNA]
Glossary: N7-methylguanosine 5'-diphosphate = m7GDP
Other name(s): Dcp2; NUDT16; D10 protein; D9 protein; D10 decapping enzyme; decapping enzyme; m7GpppN-mRNA hydrolase; m7GpppN-mRNA m7GDP phosphohydrolase
Systematic name: 5'-(N7-methylguanosine 5'-triphospho)-[mRNA] N7-methylguanosine-5'-diphosphate phosphohydrolase
Comments: Decapping of mRNA is a critical step in eukaryotic mRNA turnover. The enzyme is unable to cleave a free cap structure (m7GpppG) [3]. The enzyme from Vaccinia virus is synergistically activated in the presence of Mg2+ and Mn2+ [5].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Xu, J., Yang, J.Y., Niu, Q.W. and Chua, N.H. Arabidopsis DCP2, DCP1, and VARICOSE form a decapping complex required for postembryonic development. Plant Cell 18 (2006) 3386-3398. [PMID: 17158604]
2. Lu, G., Zhang, J., Li, Y., Li, Z., Zhang, N., Xu, X., Wang, T., Guan, Z., Gao, G.F. and Yan, J. hNUDT16: a universal decapping enzyme for small nucleolar RNA and cytoplasmic mRNA. Protein Cell 2 (2011) 64-73. [PMID: 21337011]
3. van Dijk, E., Cougot, N., Meyer, S., Babajko, S., Wahle, E. and Seraphin, B. Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures. EMBO J. 21 (2002) 6915-6924. [PMID: 12486012]
4. Parrish, S., Resch, W. and Moss, B. Vaccinia virus D10 protein has mRNA decapping activity, providing a mechanism for control of host and viral gene expression. Proc. Natl. Acad. Sci. USA 104 (2007) 2139-2144. [PMID: 17283339]
5. Souliere, M.F., Perreault, J.P. and Bisaillon, M. Characterization of the vaccinia virus D10 decapping enzyme provides evidence for a two-metal-ion mechanism. Biochem. J. 420 (2009) 27-35. [PMID: 19210265]
6. Parrish, S. and Moss, B. Characterization of a second vaccinia virus mRNA-decapping enzyme conserved in poxviruses. J. Virol. 81 (2007) 12973-12978. [PMID: 17881455]
7. Song, M.G., Li, Y. and Kiledjian, M. Multiple mRNA decapping enzymes in mammalian cells. Mol. Cell 40 (2010) 423-432. [PMID: 21070968]
Accepted name: α-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase
Reaction: α-D-ribose 1-methylphosphonate 5-triphosphate + H2O = α-D-ribose 1-methylphosphonate 5-phosphate + diphosphate
For diagram of reaction click here.
Other name(s): phnM (gene name)
Systematic name: α-D-ribose-1-methylphosphonate-5-triphosphate diphosphohydrolase
Comments: Isolated from the bacterium Escherichia coli.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Kamat, S.S., Williams, H.J. and Raushel, F.M. Intermediates in the transformation of phosphonates to phosphate by bacteria. Nature 480 (2011) 570-573. [PMID: 22089136]
Accepted name: inosine diphosphate phosphatase
Reaction: (1) IDP + H2O = IMP + phosphate
(2) dIDP + H2O = dIMP + phosphate
Other name(s): (deoxy)inosine diphosphatase; NUDT16
Systematic name: inosine diphosphate phosphatase
Comments: The human enzyme also hydrolyses GDP and dGDP, and to a lesser extent ITP, dITP and XTP.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Iyama, T., Abolhassani, N., Tsuchimoto, D., Nonaka, M. and Nakabeppu, Y. NUDT16 is a (deoxy)inosine diphosphatase, and its deficiency induces accumulation of single-strand breaks in nuclear DNA and growth arrest. Nucleic Acids Res. 38 (2010) 4834-4843. [PMID: 20385596]
Accepted name: (d)CTP diphosphatase
Reaction: (1) CTP + H2O = CMP + diphosphate
(2) dCTP + H2O = dCMP + diphosphate
Other name(s): (d)CTP pyrophosphohydrolase; (d)CTP diphosphohydrolase; nudG (gene name)
Systematic name: (deoxy)cytidine 5'-triphosphate diphosphohydrolase
Comments: The enzyme, characterized from the bacterium Escherichia coli, is specific for the pyrimidine nucleotides CTP and dCTP. It also acts on 5-methyl-dCTP, 5-hydroxy-dCTP and 8-hydroxy-dGTP.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. O'Handley, S.F., Dunn, C.A. and Bessman, M.J. Orf135 from Escherichia coli is a Nudix hydrolase specific for CTP, dCTP, and 5-methyl-dCTP. J. Biol. Chem. 276 (2001) 5421-5426. [PMID: 11053429]
2. Fujikawa, K. and Kasai, H. The oxidized pyrimidine ribonucleotide, 5-hydroxy-CTP, is hydrolyzed efficiently by the Escherichia coli recombinant Orf135 protein. DNA Repair (Amst.) 1 (2002) 571-576. [PMID: 12509230]
3. Kamiya, H., Iida, E. and Harashima, H. Important amino acids in the phosphohydrolase module of Escherichia coli Orf135. Biochem. Biophys. Res. Commun. 323 (2004) 1063-1068. [PMID: 15381107]
4. Iida, E., Satou, K., Mishima, M., Kojima, C., Harashima, H. and Kamiya, H. Amino acid residues involved in substrate recognition of the Escherichia coli Orf135 protein. Biochemistry 44 (2005) 5683-5689. [PMID: 15823026]
Accepted name: XTP/dITP diphosphatase
Reaction: (1) XTP + H2O = XMP + diphosphate
(2) dITP + H2O = dIMP + diphosphate
(3) ITP + H2O = IMP + diphosphate
Other name(s): hypoxanthine/xanthine dNTP pyrophosphatase; rdgB (gene name)
Systematic name: XTP/dITP diphosphohydrolase (diphosphate-forming)
Comments: The enzymes from the bacterium Escherichia coli and the archaea Methanococcus jannaschii and Archaeoglobus fulgidus are highly specific for XTP, dITP and ITP. The activity is dependent on divalent cations, Mg2+ is preferred.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Chung, J.H., Back, J.H., Park, Y.I. and Han, Y.S. Biochemical characterization of a novel hypoxanthine/xanthine dNTP pyrophosphatase from Methanococcus jannaschii. Nucleic Acids Res. 29 (2001) 3099-3107. [PMID: 11452035]
2. Chung, J.H., Park, H.Y., Lee, J.H. and Jang, Y. Identification of the dITP- and XTP-hydrolyzing protein from Escherichia coli. J. Biochem. Mol. Biol. 35 (2002) 403-408. [PMID: 12297000]
Accepted name: dihydroneopterin triphosphate diphosphatase
Reaction: 7,8-dihydroneopterin 3'-triphosphate + H2O = 7,8-dihydroneopterin 3'-phosphate + diphosphate
Other name(s): folQ (gene name); nudB (gene name); NUDT1 (gene name); dihydroneopterin triphosphate pyrophosphohydrolase
Systematic name: 7,8-dihydroneopterin 3'-triphosphate diphosphohydrolase
Comments: The enzyme participates in a folate biosynthesis pathway, which is found in bacteria, fungi, and plants. Requires Mg2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Suzuki, Y. and Brown, G.M. The biosynthesis of folic acid. XII. Purification and properties of dihydroneopterin triphosphate pyrophosphohydrolase. J. Biol. Chem. 249 (1974) 2405-2410. [PMID: 4362677]
2. O'Handley, S.F., Frick, D.N., Bullions, L.C., Mildvan, A.S. and Bessman, M.J. Escherichia coli orf17 codes for a nucleoside triphosphate pyrophosphohydrolase member of the MutT family of proteins. Cloning, purification, and characterization of the enzyme. J. Biol. Chem. 271 (1996) 24649-24654. [PMID: 8798731]
3. Klaus, S.M., Wegkamp, A., Sybesma, W., Hugenholtz, J., Gregory, J.F., 3rd and Hanson, A.D. A nudix enzyme removes pyrophosphate from dihydroneopterin triphosphate in the folate synthesis pathway of bacteria and plants. J. Biol. Chem. 280 (2005) 5274-5280. [PMID: 15611104]
4. Gabelli, S.B., Bianchet, M.A., Xu, W., Dunn, C.A., Niu, Z.D., Amzel, L.M. and Bessman, M.J. Structure and function of the E. coli dihydroneopterin triphosphate pyrophosphatase: a Nudix enzyme involved in folate biosynthesis. Structure 15 (2007) 1014-1022. [PMID: 17698004]
Accepted name: geranyl diphosphate phosphohydrolase
Reaction: geranyl diphosphate + H2O = geranyl phosphate + phosphate
For diagram of reaction click here.
Other name(s): NUDX1 (gene name)
Systematic name: geranyl-diphosphate phosphohydrolase
Comments: The enzyme, characterized from roses, is involved in a cytosolic pathway for the biosynthesis of free monoterpene alcohols that contribute to fragrance. In vitro the enzyme also acts on (2E,6E)-farnesyl diphosphate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Magnard, J.L., Roccia, A., Caissard, J.C., Vergne, P., Sun, P., Hecquet, R., Dubois, A., Hibrand-Saint Oyant, L., Jullien, F., Nicole, F., Raymond, O., Huguet, S., Baltenweck, R., Meyer, S., Claudel, P., Jeauffre, J., Rohmer, M., Foucher, F., Hugueney, P., Bendahmane, M. and Baudino, S. Plant volatiles. Biosynthesis of monoterpene scent compounds in roses. Science 349 (2015) 81-83. [PMID: 26138978]
Accepted name: 8-oxo-(d)GTP phosphatase
Reaction: (1) 8-oxo-GTP + H2O = 8-oxo-GDP + phosphate
(2) 8-oxo-dGTP + H2O = 8-oxo-dGDP + phosphate
Glossary: 8-oxo-dGTP = 2'-deoxy-7,8-dihydro-8-oxoguanosine 5'-triphosphate
Other name(s): mutT1 (gene name)
Systematic name: 8-oxo-dGTP diphosphohydrolase
Comments: The enzyme, characterized from the bacterium Mycobacterium tuberculosis, catalyses the hydrolysis of both 8-oxo-GTP and 8-oxo-dGTP, thereby preventing transcriptional and translational errors caused by oxidative damage. The enzyme is highly specific. Unlike EC 3.6.1.55, 8-oxo-dGTP diphosphatase, it removes only a single phosphate group. The nucleoside diphosphate products are hydrolysed further by EC 3.6.1.58, 8-oxo-dGDP phosphatase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Patil, A.G., Sang, P.B., Govindan, A. and Varshney, U. Mycobacterium tuberculosis MutT1 (Rv2985) and ADPRase (Rv1700) proteins constitute a two-stage mechanism of 8-oxo-dGTP and 8-oxo-GTP detoxification and adenosine to cytidine mutation avoidance. J. Biol. Chem 288 (2013) 11252-11262. [PMID: 23463507]
Accepted name: guanosine-5'-diphospho-5'-[DNA] diphosphatase
Reaction: guanosine-5'-diphospho-5'-[DNA] + H2O = phospho-5'-[DNA] + GMP
Other name(s): aprataxin; pp5'G5'DNA diphosphatase; pp5'G5'-DNA guanylate hydrolase; APTX (gene name); HNT3 (gene name)
Systematic name: guanosine-5'-diphospho-5'-[DNA] hydrolase (guanosine 5'-phosphate-forming)
Comments: Aprataxin is a DNA-binding protein that catalyses (among other activities) the 5' decapping of Gpp-DNA (formed by homologs of RtcB3 from the bacterium Myxococcus xanthus). The enzyme binds the guanylate group to a histidine residue at its active site, forming a covalent enzyme-nucleotide phosphate intermediate, followed by the hydrolysis of the guanylate from the nucleic acid and eventual release. The enzyme forms a 5'-phospho terminus that can be efficiently joined by "classical" ligases. The enzyme also possesses the activitiy of EC 3.6.1.71, adenosine-5'-diphospho-5'-[DNA] diphosphatase and EC 3.6.1.72, DNA-3'-diphospho-5'-guanosine diphosphatase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Maughan, W.P. and Shuman, S. Characterization of 3'-phosphate RNA ligase paralogs RtcB1, RtcB2, and RtcB3 from Myxococcus xanthus highlights DNA and RNA 5'-phosphate capping activity of RtcB3. J. Bacteriol. 197 (2015) 3616-3624. [PMID: 26350128]
Accepted name: adenosine-5'-diphospho-5'-[DNA] diphosphatase
Reaction: (1) adenosine-5'-diphospho-5'-[DNA] + H2O = AMP + phospho-5'-[DNA]
(2) adenosine-5'-diphospho-5'-(ribonucleotide)-[DNA] + H2O = AMP + 5'-phospho-(ribonucleotide)-[DNA]
Other name(s): aprataxin; 5'-App5'-DNA adenylate hydrolase; APTX (gene name); HNT3 (gene name)
Systematic name: adenosine-5'-diphospho-5'-[DNA] hydrolase (adenosine 5'-phosphate-forming)
Comments: Aprataxin is a DNA-binding protein involved in different types of DNA break repair. The enzyme acts (among other activities) on abortive DNA ligation intermediates that contain an adenylate covalently linked to the 5'-phosphate DNA terminus. It also acts when the adenylate is covalently linked to the 5'-phosphate of a ribonucleotide linked to a DNA strand, which is the result of abortive ligase activty on products of EC 3.1.26.4, ribonuclease H, an enzyme that cleaves RNA-DNA hybrids on the 5' side of the ribonucleotide found in the 5'-RNA-DNA-3' junction. Aprataxin binds the adenylate group to a histidine residue within the active site, followed by its hydrolysis from the nucleic acid and eventual release, leaving a 5'-phosphate terminus that can be efficiently rejoined. The enzyme also possesses the activities of EC 3.6.1.70, guanosine-5'-diphospho-5'-[DNA] diphosphatase, and EC 3.6.1.72, DNA-3'-diphospho-5'-guanosine diphosphatase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Ahel, I., Rass, U., El-Khamisy, S.F., Katyal, S., Clements, P.M., McKinnon, P.J., Caldecott, K.W. and West, S.C. The neurodegenerative disease protein aprataxin resolves abortive DNA ligation intermediates. Nature 443 (2006) 713-716. [PMID: 16964241]
2. Tumbale, P., Williams, J.S., Schellenberg, M.J., Kunkel, T.A. and Williams, R.S. Aprataxin resolves adenylated RNA-DNA junctions to maintain genome integrity. Nature 506 (2014) 111-115. [PMID: 24362567]
Accepted name: DNA-3'-diphospho-5'-guanosine diphosphatase
Reaction: [DNA]-3'-diphospho-5'-guanosine + H2O = [DNA]-3'-phosphate + GMP
Other name(s): aprataxin; DNA-3'pp5'G guanylate hydrolase; APTX (gene name); HNT3 (gene name)
Systematic name: [DNA]-3'-diphospho-5'-guanosine hydrolase (guanosine 5'-phosphate-forming)
Comments: Aprataxin is a DNA-binding protein that catalyses (among other activities) the 3' decapping of DNA-ppG (formed by EC 6.5.1.8, 3'-phosphate/5'-hydroxy nucleic acid ligase) [1]. The enzyme binds the guanylate group to a histidine residue at its active site, forming a covalent enzyme-nucleotide phosphate intermediate, followed by the hydrolysis of the guanylate from the nucleic acid and its eventual release. The enzyme also possesses the activity of EC 3.6.1.71, adenosine-5'-diphospho-5'-[DNA] diphosphatase, and EC 3.6.1.70, guanosine-5'-diphospho-5'-[DNA] diphosphatase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Das, U., Chauleau, M., Ordonez, H. and Shuman, S. Impact of DNA3'pp5'G capping on repair reactions at DNA 3' ends. Proc. Natl. Acad. Sci. USA 111 (2014) 11317-11322. [PMID: 25049385]
2. Chauleau, M., Jacewicz, A. and Shuman, S. DNA3'pp5'G de-capping activity of aprataxin: effect of cap nucleoside analogs and structural basis for guanosine recognition. Nucleic Acids Res. 43 (2015) 6075-6083. [PMID: 26007660]
Accepted name: inosine/xanthosine triphosphatase
Reaction: (1) inosine 5'-triphosphate + H2O = inosine 5'-diphosphate + phosphate
(2) xanthosine 5'-triphosphate + H2O = xanthosine 5'-diphosphate + phosphate
Glossary: inosine 5'-triphosphate = ITP
xanthosine 5'-triphosphate = XTP
Other name(s): yjjX (gene name)
Systematic name: inosine/xanthosine 5'-triphosphate phosphohydrolase
Comments: The enzyme, characterized from the bacterium Escherichia coli, preferentially hydrolyses inosine triphosphate and xanthosine triphosphate, which are formed by oxidative deamination damage. By hydrolysing these damaged nucleotides, the enzyme prevents their incorporation into RNA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Zheng, J., Singh, V.K. and Jia, Z. Identification of an ITPase/XTPase in Escherichia coli by structural and biochemical analysis. Structure 13 (2005) 1511-1520. [PMID: 16216582]
Accepted name: mRNA 5'-phosphatase
Reaction: a 5'-triphospho-[mRNA] + H2O = a 5'-diphospho-[mRNA] + phosphate
Other name(s): 5'-polynucleotidase; polynucleotide 5'-phosphohydrolase; RNGTT (gene name); CET1 (gene name); mRNA 5′-triphosphate monophosphatase
Systematic name: 5'-triphospho-mRNA 5'-phosphohydrolase
Comments: The enzyme, found in eukaryotes and some plus strand RNA viruses (e.g. alphavirus), is involved in mRNA capping. Unlike the eukaryotic enzyme, the viral enzyme requires a purine in the first position of the mRNA. The human enzyme is a multi domain protein that also has the activity of EC 2.7.7.50, mRNA guanylyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Itoh, N., Mizumoto, K. and Kaziro, Y. Messenger RNA guanlyltransferase from Saccharomyces cerevisiae. II. Catalytic properties. J. Biol. Chem. 259 (1984) 13930-13936. [PMID: 6094533]
2. Tsukamoto, T., Shibagaki, Y., Murakoshi, T., Suzuki, M., Nakamura, A., Gotoh, H. and Mizumoto, K. Cloning and characterization of two human cDNAs encoding the mRNA capping enzyme. Biochem. Biophys. Res. Commun. 243 (1998) 101-108. [PMID: 9473487]
3. Vasiljeva, L., Merits, A., Auvinen, P. and Kaariainen, L. Identification of a novel function of the alphavirus capping apparatus. RNA 5'-triphosphatase activity of Nsp2. J. Biol. Chem. 275 (2000) 17281-17287. [PMID: 10748213]
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]
Accepted name: prenyl-diphosphate phosphatase
Reaction: (1) prenyl diphosphate + H2O = prenyl phosphate + phosphate
(2) 3-methylbut-3-en-1-yl diphosphate + H2O = 3-methylbut-3-en-1-yl phosphate + phosphate
Glossary: isopentenyl = 3-methylbut-3-en-1-yl
prenyl = 3-methylbut-2-en-1-yl = dimethylallyl
dimethylallyl diphosphate = DMAPP
isopentenyl diphosphate = IPP
Systematic name: prenyl diphosphate/3-methylbut-3-en-1-yl diphosphate phosphohydrolase
Comments: The enzyme, characterized from the methanogenic archaeon Methanosarcina mazei, belongs to the Nudix hydrolase family (a superfamily of hydrolytic enzymes capable of cleaving nucleoside diphosphates linked to a moiety). Its main purpose is to provide the substrate for EC 2.5.1.129, flavin prenyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Ishibashi, Y., Matsushima, N., Ito, T. and Hemmi, H. Isopentenyl diphosphate/dimethylallyl diphosphate-specific Nudix hydrolase from the methanogenic archaeon Methanosarcina mazei. Biosci. Biotechnol. Biochem. 86 (2022) 246-253. [PMID: 34864834]
Accepted name: coenzyme A diphosphatase
Reaction: coenzyme A + H2O = adenosine 3',5'-bisphosphate + 4'-phosphopantetheine
Other name(s): CoA pyrophosphatase; coenzyme A pyrophosphatase; CoA diphosphohydrolase; Nudt19; Nudt7; thnR (gene name)
Systematic name: coenzyme A 4'-phosphopantetheine phosphohydrolase
Comments: The enzyme belongs to the Nudix hydrolase family. It has been reported from bacteria, yeast, and mammals. Activity is higher with oxidized disulfide CoA than with reduced CoA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Xu, W., Shen, J., Dunn, C.A., Desai, S. and Bessman, M.J. The Nudix hydrolases of Deinococcus radiodurans. Mol. Microbiol. 39 (2001) 286-290. [PMID: 11136450]
2. Gasmi, L. and McLennan, A.G. The mouse Nudt7 gene encodes a peroxisomal nudix hydrolase specific for coenzyme A and its derivatives. Biochem. J. 357 (2001) 33-38. [PMID: 11415433]
3. Kang, L.W., Gabelli, S.B., Bianchet, M.A., Xu, W.L., Bessman, M.J. and Amzel, L.M. Structure of a coenzyme A pyrophosphatase from Deinococcus radiodurans: a member of the Nudix family. J. Bacteriol. 185 (2003) 4110-4118. [PMID: 12837785]
4. Freeman, M.F., Moshos, K.A., Bodner, M.J., Li, R. and Townsend, C.A. Four enzymes define the incorporation of coenzyme A in thienamycin biosynthesis. Proc. Natl. Acad. Sci. USA 105 (2008) 11128-11133. [PMID: 18678912]
5. Shumar, S.A., Kerr, E.W., Geldenhuys, W.J., Montgomery, G.E., Fagone, P., Thirawatananond, P., Saavedra, H., Gabelli, S.B. and Leonardi, R. Nudt19 is a renal CoA diphosphohydrolase with biochemical and regulatory properties that are distinct from the hepatic Nudt7 isoform. J. Biol. Chem. 293 (2018) 4134-4148. [PMID: 29378847]
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, Metacyc, PDB, 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
Glossary: 3'-phosphoadenylyl sulfate = PAPS
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, Metacyc, 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.