The Enzyme Database

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EC 2.7.11.5     
Accepted name: [isocitrate dehydrogenase (NADP+)] kinase
Reaction: ATP + [isocitrate dehydrogenase (NADP+)] = ADP + [isocitrate dehydrogenase (NADP+)] phosphate
Other name(s): [isocitrate dehydrogenase (NADP)] kinase; ICDH kinase/phosphatase; IDH kinase; IDH kinase/phosphatase; IDH-K/P; IDHK/P; isocitrate dehydrogenase kinase (phosphorylating); isocitrate dehydrogenase kinase/phosphatase; STK3
Systematic name: ATP:[isocitrate dehydrogenase (NADP+)] phosphotransferase
Comments: The enzyme has no activating compound but is specific for its substrate. Phosphorylates and inactivates EC 1.1.1.42, isocitrate dehydrogenase (NADP+).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 83682-93-3
References:
1.  Wang, J.Y.J. and Koshland, D.E., Jr. The reversible phosphorylation of isocitrate dehydrogenase of Salmonella typhimurium. Arch. Biochem. Biophys. 218 (1982) 59–67. [PMID: 6756316]
2.  Miller, S.P., Karschnia, E.J., Ikeda, T.P. and LaPorte, D.C. Isocitrate dehydrogenase kinase/phosphatase. Kinetic characteristics of the wild-type and two mutant proteins. J. Biol. Chem. 271 (1996) 19124–19128. [PMID: 8702587]
3.  Singh, S.K., Matsuno, K., LaPorte, D.C. and Banaszak, L.J. Crystal structure of Bacillus subtilis isocitrate dehydrogenase at 1.55 Å. Insights into the nature of substrate specificity exhibited by Escherichia coli isocitrate dehydrogenase kinase/phosphatase. J. Biol. Chem. 276 (2001) 26154–26163. [PMID: 11290745]
4.  Oudot, C., Cortay, J.C., Blanchet, C., Laporte, D.C., Di Pietro, A., Cozzone, A.J. and Jault, J.M. The "catalytic" triad of isocitrate dehydrogenase kinase/phosphatase from E. coli and its relationship with that found in eukaryotic protein kinases. Biochemistry 40 (2001) 3047–3055. [PMID: 11258918]
[EC 2.7.11.5 created 1986 as EC 2.7.1.116, transferred 2005 to EC 2.7.11.5]
 
 


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