The Enzyme Database

Your query returned 3 entries.    printer_iconPrintable version



EC 2.7.3.8     
Accepted name: ammonia kinase
Reaction: ATP + NH3 = ADP + phosphoramide
Other name(s): phosphoramidate-adenosine diphosphate phosphotransferase; phosphoramidate-ADP-phosphotransferase
Systematic name: ATP:ammonia phosphotransferase
Comments: Has a wide specificity. In the reverse direction, N-phosphoglycine and N-phosphohistidine can also act as phosphate donors, and ADP, dADP, GDP, CDP, dTDP, dCDP, IDP and UDP can act as phosphate acceptors (in decreasing order of activity).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37278-16-3
References:
1.  Dowler, M.J. and Nakada, H.I. Yeast phosphoramidate-adenosine diphosphate phosphotransferase. J. Biol. Chem. 243 (1968) 1434–1440. [PMID: 5647264]
[EC 2.7.3.8 created 1972]
 
 
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]
[EC 2.7.4.19 created 1984]
 
 
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
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]
[EC 2.7.4.25 created 2011]
 
 


Data © 2001–2021 IUBMB
Web site © 2005–2021 Andrew McDonald