EC |
2.1.1.54 |
Accepted name: |
deoxycytidylate C-methyltransferase |
Reaction: |
5,10-methylenetetrahydrofolate + dCMP = dihydrofolate + deoxy-5-methylcytidylate |
Other name(s): |
deoxycytidylate methyltransferase; dCMP methyltransferase |
Systematic name: |
5,10-methylenetetrahydrofolate:dCMP C-methyltransferase |
Comments: |
dCMP is methylated by formaldehyde in the presence of tetrahydrofolate. CMP, dCTP and CTP can act as acceptors, but more slowly. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 61970-01-2 |
References: |
1. |
Kuo, T.-T. and Tu, J. Enzymatic synthesis of deoxy-5-methyl-cytidylic acid replacing deoxycytidylic acid in Xanthomonas oryzae phage Xp12DNA. Nature 263 (1976) 615. [PMID: 980110] |
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[EC 2.1.1.54 created 1978] |
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|
EC |
2.1.2.8 |
Accepted name: |
deoxycytidylate 5-hydroxymethyltransferase |
Reaction: |
5,10-methylenetetrahydrofolate + H2O + deoxycytidylate = tetrahydrofolate + 5-hydroxymethyldeoxycytidylate |
Other name(s): |
dCMP hydroxymethylase; d-cytidine 5′-monophosphate hydroxymethylase; deoxyCMP hydroxymethylase; deoxycytidylate hydroxymethylase; deoxycytidylic hydroxymethylase |
Systematic name: |
5,10-methylenetetrahydrofolate:deoxycytidylate 5-hydroxymethyltransferase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9012-68-4 |
References: |
1. |
Mathews, C.K., Brown, F. and Cohen, S.S. Virus-induced acquisition of metabolic function. VII. Biosynthesis de novo of deoxycytidylate hydroxymethylase. J. Biol. Chem. 239 (1964) 2957–2963. [PMID: 14217882] |
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[EC 2.1.2.8 created 1972] |
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EC |
2.7.1.74 |
Accepted name: |
deoxycytidine kinase |
Reaction: |
NTP + deoxycytidine = NDP + dCMP |
Other name(s): |
deoxycytidine kinase (phosphorylating); 2′-deoxycytidine kinase; Ara-C kinase; arabinofuranosylcytosine kinase; deoxycytidine-cytidine kinase |
Systematic name: |
NTP:deoxycytidine 5′-phosphotransferase |
Comments: |
Cytosine arabinoside can act as acceptor; all natural nucleoside triphosphates (except dCTP) can act as donors. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9039-45-6 |
References: |
1. |
Durham, J.P. and Ives, D.H. Deoxycytidine kinase. II. Purification and general properties of the calf thymus enzyme. J. Biol. Chem. 245 (1970) 2276–2284. [PMID: 5442271] |
2. |
Ives, D.H. and Durham, J.P. Deoxycytidine kinase. 3. Kinetics and allosteric regulation of the calf thymus enzyme. J. Biol. Chem. 245 (1970) 2285–2294. [PMID: 5462538] |
3. |
Kessel, D. Properties of deoxycytidine kinase partially purified from L1210 cells. J. Biol. Chem. 243 (1968) 4739–4744. [PMID: 5687717] |
4. |
Momparler, R.L. and Fischer, G.A. Mammalian deoxynucleoside kinase. I. Deoxycytidine kinase: purification, properties, and kinetic studies with cytosine arabinoside. J. Biol. Chem. 243 (1968) 4298–4304. [PMID: 5684726] |
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[EC 2.7.1.74 created 1972] |
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EC |
2.7.4.14 |
Accepted name: |
UMP/CMP kinase |
Reaction: |
(1) ATP + (d)CMP = ADP + (d)CDP (2) ATP + UMP = ADP + UDP |
Other name(s): |
cytidylate kinase (misleading); deoxycytidylate kinase (misleading); CTP:CMP phosphotransferase (misleading); dCMP kinase (misleading); deoxycytidine monophosphokinase (misleading); UMP-CMP kinase; ATP:UMP-CMP phosphotransferase; pyrimidine nucleoside monophosphate kinase; uridine monophosphate-cytidine monophosphate phosphotransferase |
Systematic name: |
ATP:(d)CMP/UMP phosphotransferase |
Comments: |
This eukaryotic enzyme is a bifunctional enzyme that catalyses the phosphorylation of both CMP and UMP with similar efficiency. dCMP can also act as acceptor. Different from the monofunctional prokaryotic enzymes EC 2.7.4.25, (d)CMP kinase and EC 2.7.4.22, UMP kinase. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 37278-21-0 |
References: |
1. |
Hurwitz, J. The enzymatic incorporation of ribonucleotides into polydeoxynucleotide material. J. Biol. Chem. 234 (1959) 2351–2358. [PMID: 14405566] |
2. |
Ruffner, B.W., Jr. and Anderson, E.P. Adenosine triphosphate: uridine monophosphate-cytidine monophosphate phosphotransferase from Tetrahymena pyriformis. J. Biol. Chem. 244 (1969) 5994–6002. [PMID: 5350952] |
3. |
Scheffzek, K., Kliche, W., Wiesmuller, L. and Reinstein, J. Crystal structure of the complex of UMP/CMP kinase from Dictyostelium discoideum and the bisubstrate inhibitor P1-(5′-adenosyl) P5-(5′-uridyl) pentaphosphate (UP5A) and Mg2+ at 2.2 Å: implications for water-mediated specificity. Biochemistry 35 (1996) 9716–9727. [DOI] [PMID: 8703943] |
4. |
Zhou, L., Lacroute, F. and Thornburg, R. Cloning, expression in Escherichia coli, and characterization of Arabidopsis thaliana UMP/CMP kinase. Plant Physiol. 117 (1998) 245–254. [PMID: 9576794] |
5. |
Van Rompay, A.R., Johansson, M. and Karlsson, A. Phosphorylation of deoxycytidine analog monophosphates by UMP-CMP kinase: molecular characterization of the human enzyme. Mol. Pharmacol. 56 (1999) 562–569. [PMID: 10462544] |
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[EC 2.7.4.14 created 1961 as EC 2.7.4.5, transferred 1972 to EC 2.7.4.14, modified 1980, modified 2011] |
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EC |
2.7.4.19 |
Accepted name: |
5-methyldeoxycytidine-5′-phosphate kinase |
Reaction: |
ATP + 5-methyldeoxycytidine 5′-phosphate = ADP + 5-methyldeoxycytidine diphosphate |
Systematic name: |
ATP:5-methyldeoxycytidine-5′-phosphate phosphotransferase |
Comments: |
The enzyme, from phage XP-12-infected Xanthomonas oryzae, converts m5dCMP into m5dCDP and then into m5dCTP. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 81032-53-3 |
References: |
1. |
Wang, R.Y.-H., Huang, L.-H. and Ehrlich, M. A bacteriophage-induced 5-methyldeoxycytidine 5′-monophosphate kinase. Biochim. Biophys. Acta 696 (1982) 31–36. [DOI] [PMID: 7082669] |
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[EC 2.7.4.19 created 1984] |
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EC |
2.7.4.25 |
Accepted name: |
(d)CMP kinase |
Reaction: |
ATP + (d)CMP = ADP + (d)CDP |
Glossary: |
CMP = cytidine monophosphate
dCMP = deoxycytidine monophosphate
CDP = cytidine diphosphate
dCDP = deoxycytidine diphosphate
UMP = uridine monophosphate
UDP = uridine diphosphate |
Other name(s): |
cmk (gene name); prokaryotic cytidylate kinase; deoxycytidylate kinase (misleading); dCMP kinase (misleading); deoxycytidine monophosphokinase (misleading) |
Systematic name: |
ATP:(d)CMP phosphotransferase |
Comments: |
The prokaryotic cytidine monophosphate kinase specifically phosphorylates CMP (or dCMP), using ATP as the preferred phosphoryl donor. Unlike EC 2.7.4.14, a eukaryotic enzyme that phosphorylates UMP and CMP with similar efficiency, the prokaryotic enzyme phosphorylates UMP with very low rates, and this function is catalysed in prokaryotes by EC 2.7.4.22, UMP kinase. The enzyme phosphorylates dCMP nearly as well as it does CMP [1]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Bertrand, T., Briozzo, P., Assairi, L., Ofiteru, A., Bucurenci, N., Munier-Lehmann, H., Golinelli-Pimpaneau, B., Barzu, O. and Gilles, A.M. Sugar specificity of bacterial CMP kinases as revealed by crystal structures and mutagenesis of Escherichia coli enzyme. J. Mol. Biol. 315 (2002) 1099–1110. [DOI] [PMID: 11827479] |
2. |
Thum, C., Schneider, C.Z., Palma, M.S., Santos, D.S. and Basso, L.A. The Rv1712 Locus from Mycobacterium tuberculosis H37Rv codes for a functional CMP kinase that preferentially phosphorylates dCMP. J. Bacteriol. 191 (2009) 2884–2887. [DOI] [PMID: 19181797] |
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[EC 2.7.4.25 created 2011] |
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EC |
3.1.3.35 |
Accepted name: |
thymidylate 5′-phosphatase |
Reaction: |
thymidylate + H2O = thymidine + phosphate |
Other name(s): |
thymidylate 5′-nucleotidase; deoxythymidylate 5′-nucleotidase; thymidylate nucleotidase; deoxythymidylic 5′-nucleotidase; deoxythymidylate phosphohydrolase; dTMPase |
Systematic name: |
thymidylate 5′-phosphohydrolase |
Comments: |
Acts on 5-methyl-dCMP and on TMP, but more slowly than on dTMP. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9026-80-6 |
References: |
1. |
Aposhian, H.V. and Tremblay, G.Y. Deoxythymidylate 5′-nucleotidase. Purification and properties of an enzyme found after infection of Bacillus subtilis with phage SP5C. J. Biol. Chem. 241 (1966) 5095–5101. [PMID: 4958986] |
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[EC 3.1.3.35 created 1972] |
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EC |
3.2.2.10 |
Accepted name: |
pyrimidine-5′-nucleotide nucleosidase |
Reaction: |
a pyrimidine 5′-nucleotide + H2O = D-ribose 5-phosphate + a pyrimidine base |
Other name(s): |
pyrimidine nucleotide N-ribosidase; Pyr5N |
Systematic name: |
pyrimidine-5′-nucleotide phosphoribo(deoxyribo)hydrolase |
Comments: |
Also acts on dUMP, dTMP and dCMP. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9023-31-8 |
References: |
1. |
Imada, A. Degradation of pyrimidine nucleotides by enzyme systems of Streptomyces. II. Pyrimidine 5′-nucleotide phosphoribo(deoxyribo) hydrolase of Streptomyces virginiae. J. Gen. Appl. Microbiol. 13 (1967) 267–278. |
2. |
Imada, A., Kuno, M. and Igarasi, S. Degradation of pyrimidine nucleotides by enzyme systems of Streptomyces. I. Ribose-5-phosphate formation from pyrimidine nucleotides. J. Gen. Appl. Microbiol. 13 (1967) 255–265. |
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[EC 3.2.2.10 created 1972] |
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EC |
3.5.4.12 |
Accepted name: |
dCMP deaminase |
Reaction: |
dCMP + H2O = dUMP + NH3 |
Other name(s): |
deoxycytidylate deaminase; deoxy-CMP-deaminase; deoxycytidylate aminohydrolase; deoxycytidine monophosphate deaminase; deoxycytidine-5′-phosphate deaminase; deoxycytidine-5′-monophosphate aminohydrolase |
Systematic name: |
dCMP aminohydrolase |
Comments: |
Also acts on some 5-substituted dCMPs. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9026-92-0 |
References: |
1. |
Scarano, E. The enzymatic deamination of 6-aminopyrimidine deoxyribonucleotides. I. The enzymatic deamination of deoxycytidine 5′-phosphate and of 5-methyldeoxycytidine 5-methyldeoxycytidine 5′-phosphate. J. Biol. Chem. 235 (1960) 706–713. [PMID: 14442222] |
2. |
Scarano, E., Bonaduce, L. and de Petrocellis, B. The enzymatic deamination of 6-aminopyrimidine deoxyribonucleotides. II. Purification and properties of a 6-aminopyrimidine deoxyribonucleoside 5′-phosphate deaminase from unfertilized eggs of sea urchin. J. Biol. Chem. 235 (1960) 3556–3561. [PMID: 13747062] |
3. |
Sergott, R.C., Debeer, L.J. and Bessman, M.J. On the regulation of a bacterial deoxycytidylate deaminase. J. Biol. Chem. 246 (1971) 7755–7758. [PMID: 5002683] |
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[EC 3.5.4.12 created 1965] |
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EC |
3.5.4.30 |
Accepted name: |
dCTP deaminase (dUMP-forming) |
Reaction: |
dCTP + 2 H2O = dUMP + diphosphate + NH3 |
Systematic name: |
dCTP aminohydrolase (dUMP-forming) |
Comments: |
Requires Mg2+. Is highly specific for dCTP as substrate as dCMP, CTP, CDP, CMP, cytosine or deoxycytosine are not deaminated. While most bacteria require two enzymes to form dUMP from dCTP (EC 3.5.4.13, dCTP deaminase and EC 3.6.1.23, dUTP diphosphatase), the archaeon Methanocaldococcus jannaschii uses a single enzyme to carry out both functions. This enzyme can also act as a dUTP diphosphatase, but more slowly. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Li, H., Xu, H., Graham, D.E. and White, R.H. The Methanococcus jannaschii dCTP deaminase is a bifunctional deaminase and diphosphatase. J. Biol. Chem. 278 (2003) 11100–11106. [DOI] [PMID: 12538648] |
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[EC 3.5.4.30 created 2003] |
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EC |
3.6.1.12 |
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. [PMID: 13788541] |
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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 24467396] |
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[EC 3.6.1.12 created 1965] |
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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, PDB |
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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 15823026] |
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[EC 3.6.1.65 created 2013] |
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