Enzyme Nomenclature

Continued from EC 3.5.4 to EC 3.5.99

EC 3.6

Acting on Acid Anhydrides

Sections

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


EC 3.6.1 In Phosphorus-Containing Anhydrides

Contents

EC 3.6.1.1 inorganic diphosphatase
EC 3.6.1.2 trimetaphosphatase
EC 3.6.1.3 adenosinetriphosphatase
EC 3.6.1.4 deleted, included in EC 3.6.1.3
EC 3.6.1.5 apyrase
EC 3.6.1.6 nucleoside diphosphate phosphatase
EC 3.6.1.7 acylphosphatase
EC 3.6.1.8 ATP diphosphatase
EC 3.6.1.9 nucleotide diphosphatase
EC 3.6.1.10 endopolyphosphatase
EC 3.6.1.11 exopolyphosphatase
EC 3.6.1.12 dCTP diphosphatase
EC 3.6.1.13 ADP-ribose diphosphatase
EC 3.6.1.14 adenosine-tetraphosphatase
EC 3.6.1.15 nucleoside-triphosphate phosphatase
EC 3.6.1.16 CDP-glycerol diphosphatase
EC 3.6.1.17 bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)
EC 3.6.1.18 FAD diphosphatase
EC 3.6.1.19 nucleoside-triphosphate diphosphatase
EC 3.6.1.19 now included in *EC 3.6.1.9
EC 3.6.1.20 5'-acylphosphoadenosine hydrolase
EC 3.6.1.21 ADP-sugar diphosphatase
EC 3.6.1.22 NAD+ diphosphatase
EC 3.6.1.23 dUTP diphosphatase
EC 3.6.1.24 nucleoside phosphoacylhydrolase
EC 3.6.1.25 triphosphatase
EC 3.6.1.26 CDP-diacylglycerol diphosphatase
EC 3.6.1.27 undecaprenyl-diphosphate phosphatase
EC 3.6.1.28 thiamine-triphosphatase
EC 3.6.1.29 bis(5'-adenosyl)-triphosphatase
EC 3.6.1.30 deleted now covered by EC 3.6.1.59 and EC 3.6.1.62.
EC 3.6.1.31 phosphoribosyl-ATP diphosphatase
EC 3.6.1.32 now EC 3.6.4.1
EC 3.6.1.33 now EC 3.6.4.2
EC 3.6.1.34 now EC 3.6.3.14
EC 3.6.1.35 now EC 3.6.3.6
EC 3.6.1.36 now EC 3.6.3.10
EC 3.6.1.37 now EC 3.6.3.9
EC 3.6.1.38 now EC 3.6.3.8
EC 3.6.1.39 thymidine-triphosphatase
EC 3.6.1.40 guanosine-5'-triphosphate,3'-diphosphate phosphatase
EC 3.6.1.41 bis(5'-nucleosyl)-tetraphosphatase (symmetrical)
EC 3.6.1.42 guanosine-diphosphatase
EC 3.6.1.43 dolichyldiphosphatase
EC 3.6.1.44 oligosaccharide-diphosphodolichol diphosphatase
EC 3.6.1.45 UDP-sugar diphosphatase
EC 3.6.1.46 heterotrimeric G-protein GTPase
EC 3.6.1.47 small monomeric GTPase
EC 3.6.1.48 protein-synthesizing GTPase
EC 3.6.1.49 signal-recognition-particle GTPase
EC 3.6.1.50 dynamin GTPase
EC 3.6.1.51 tubulin GTPase
EC 3.6.1.46 now EC 3.6.5.1
EC 3.6.1.47 now EC 3.6.5.2
EC 3.6.1.48 now EC 3.6.5.3
EC 3.6.1.49 now EC 3.6.5.4
EC 3.6.1.50 now EC 3.6.5.5
EC 3.6.1.51 now EC 3.6.5.6
EC 3.6.1.52 diphosphoinositol-polyphosphate diphosphatase
EC 3.6.1.53 Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase
EC 3.6.1.54 UDP-2,3-diacylglucosamine diphosphatase
EC 3.6.1.55 8-oxo-dGTP diphosphatase
EC 3.6.1.56 2-hydroxy-dATP diphosphatase
EC 3.6.1.57 UDP-2,4-diacetamido-2,4,6-trideoxy-β-L-altropyranose hydrolase
EC 3.6.1.58 8-oxo-dGDP phosphatase
EC 3.6.1.59 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase
EC 3.6.1.60 diadenosine hexaphosphate hydrolase (AMP-forming)
EC 3.6.1.61 diadenosine hexaphosphate hydrolase (ATP-forming)
EC 3.6.1.62 5'-(N7-methylguanosine 5'-triphospho)-[mRNA] hydrolase
EC 3.6.1.63 α-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase
EC 3.6.1.64 inosine diphosphate phosphatase
EC 3.6.1.65 (d)CTP diphosphatase
EC 3.6.1.66 XTP/dITP diphosphatase
EC 3.6.1.67 dihydroneopterin triphosphate diphosphatase
EC 3.6.1.68 geranyl diphosphate phosphohydrolase


Entries

EC 3.6.1.1

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, 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.

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.

[EC 3.6.1.1 created 1961, modified 2000]

EC 3.6.1.2

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 3.6.1.2 created 1961]

EC 3.6.1.3

Accepted name: adenosinetriphosphatase

Reaction: ATP + H2O = ADP + phosphate

Other name(s): adenylpyrophosphatase; ATP monophosphatase; triphosphatase; ATPase (ambiguous); 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, Metacyc, 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 3.6.1.3 created 1961 (EC 3.6.1.4 created 1961, incorporated 1965)]

[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)]

EC 3.6.1.5

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; 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, 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]

[EC 3.6.1.5 created 1961, modified 1976, modified 2000, modified 2013]

EC 3.6.1.6

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]

[EC 3.6.1.6 created 1961]

EC 3.6.1.7

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]

[EC 3.6.1.7 created 1961]

EC 3.6.1.8

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, 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.

[EC 3.6.1.8 created 1961]

EC 3.6.1.9

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]

[EC 3.6.1.9 created 1961 (EC 3.6.1.19 created 1972, incorporated 2016), modified 2016]

EC 3.6.1.10

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.

[EC 3.6.1.10 created 1961]

EC 3.6.1.11

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.

[EC 3.6.1.11 created 1965]

EC 3.6.1.12

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, 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.

[EC 3.6.1.12 created 1965]

EC 3.6.1.13

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.

[EC 3.6.1.13 created 1965]

EC 3.6.1.14

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, 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]

[EC 3.6.1.14 created 1972]

EC 3.6.1.15

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]

[EC 3.6.1.15 created 1972]

EC 3.6.1.16

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.

[EC 3.6.1.16 created 1972]

EC 3.6.1.17

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]

[EC 3.6.1.17 created 1972, modified 1976, modified 1986]

EC 3.6.1.18

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 3.6.1.18 created 1972]

[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)]

EC 3.6.1.20

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.

[EC 3.6.1.20 created 1972]

EC 3.6.1.21

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]

[EC 3.6.1.21 created 1972, modified 1999]

EC 3.6.1.22

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]

[EC 3.6.1.22 created 1972]

EC 3.6.1.23

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, Metacyc, 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]

[EC 3.6.1.23 created 1972]

EC 3.6.1.24

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]

[EC 3.6.1.24 created 1972]

EC 3.6.1.25

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, 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.

[EC 3.6.1.25 created 1976]

EC 3.6.1.26

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]

[EC 3.6.1.26 created 1976]

EC 3.6.1.27

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, 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]

[EC 3.6.1.27 created 1978, modified 2002, modified 2012]

EC 3.6.1.28

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]

[EC 3.6.1.28 created 1978]

EC 3.6.1.29

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 3.6.1.29 created 1978]

[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)]

EC 3.6.1.31

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 3.6.1.31 created 1981]

[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)]

EC 3.6.1.39

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]

[EC 3.6.1.39 created 1984]

EC 3.6.1.40

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, 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]

[EC 3.6.1.40 created 1986, modified 2010]

EC 3.6.1.41

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]

[EC 3.6.1.41 created 1986]

EC 3.6.1.42

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, 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]

[EC 3.6.1.42 created 1989]

EC 3.6.1.43

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.

[EC 3.6.1.43 created 1989]

EC 3.6.1.44

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]

[EC 3.6.1.44 created 1992]

EC 3.6.1.45

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 3.6.1.45 created 1999]

[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)]

EC 3.6.1.52

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]

[EC 3.6.1.52 created 2002]

EC 3.6.1.53

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]

[EC 3.6.1.53 created 2008]

EC 3.6.1.54

Accepted name: UDP-2,3-diacylglucosamine diphosphatase

Reaction: UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-α-D-glucosamine + H2O = 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl ]-α-D-glucosaminyl 1-phosphate + UMP

For diagram of reaction click here.

Glossary: tetradecanoyl = myristoyl

Other name(s): UDP-2,3-diacylglucosamine hydrolase; UDP-2,3-diacylglucosamine pyrophosphatase; ybbF (gene name); lpxH (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)

Systematic name: 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

Comments: The enzyme catalyses a step in the biosynthesis of lipid A.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, 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]

[EC 3.6.1.54 created 2010]

EC 3.6.1.55

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]

[EC 3.6.1.55 created 2011]

EC 3.6.1.56

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]

[EC 3.6.1.56 created 2011]

EC 3.6.1.57

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]

[EC 3.6.1.57 created 2011]

EC 3.6.1.58

Accepted name: 8-oxo-dGDP phosphatase

Reaction: 8-oxo-dGDP + H2O = 8-oxo-dGMP + 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]

[EC 3.6.1.58 created 2012]

EC 3.6.1.59

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, 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]

[EC 3.6.1.59 created 2012, modified 2013]

EC 3.6.1.60

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]

[EC 3.6.1.60 created 2012]

EC 3.6.1.61

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, 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]

[EC 3.6.1.61 created 2012]

EC 3.6.1.62

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, 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]

[EC 3.6.1.62 created 2012, modified 2013]

EC 3.6.1.63

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]

[EC 3.6.1.63 created 2012]

EC 3.6.1.64

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, 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]

[EC 3.6.1.64 created 2013]

EC 3.6.1.65

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, 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]

[EC 3.6.1.65 created 2013]

EC 3.6.1.66

Accepted name: XTP/dITP diphosphatase

Reaction: (1) XTP + H2O = XMP + diphosphate
(2) dITP + H2O = dIMP + 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 and dITP. The activity is dependent on divalent cations, Mg2+ is preferred.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, 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]

[EC 3.6.1.66 created 2013]

EC 3.6.1.67

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, 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]

[EC 3.6.1.67 created 2014]

EC 3.6.1.68

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, 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]

[EC 3.6.1.68 created 2015 as EC 3.1.3.98, transferred 2016 to EC 3.6.1.68]


EC 3.6.2 In Sulfonyl-Containing Anhydrides

Contents

EC 3.6.2.1 adenylylsulfatase
EC 3.6.2.2 phosphoadenylylsulfatase


Entries

EC 3.6.2.1

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, 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]

[EC 3.6.2.1 created 1972]

EC 3.6.2.2

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.

[EC 3.6.2.2 created 1972]


Continued with EC 3.6.3
Return to EC 3 home page
Return to Enzymes home page
Return to IUBMB Biochemical Nomenclature home page