(isocitrate dehydrogenase (NADP+)) kinase

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In enzymology, a [isocitrate dehydrogenase (NADP+)] kinase (EC 2.7.11.5) is an enzyme that catalyzes the chemical reaction

ATP + [isocitrate dehydrogenase (NADP⁺)] $\rightleftharpoons$ ADP + [isocitrate dehydrogenase (NADP⁺)] phosphate

Thus, the two substrates of this enzyme are ATP and [[[isocitrate dehydrogenase (NADP+)]]], whereas its two products are ADP and [[[isocitrate dehydrogenase (NADP+)] phosphate]].

This enzyme belongs to the family of transferases, specifically those transferring a phosphate group to the sidechain oxygen atom of serine or threonine residues in proteins (protein-serine/threonine kinases). The systematic name of this enzyme class is ATP:[isocitrate dehydrogenase (NADP+)] phosphotransferase. Other names in common use include [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, and STK3. This enzyme participates in mapk signaling pathway.

[edit] References

IUBMB entry for 2.7.11.5
BRENDA references for 2.7.11.5 (Recommended.)
PubMed references for 2.7.11.5
PubMed Central references for 2.7.11.5
Google Scholar references for 2.7.11.5
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Miller SP, Karschnia EJ, Ikeda TP, LaPorte DC (1996). "Isocitrate dehydrogenase kinase/phosphatase. Kinetic characteristics of the wild-type and two mutant proteins". J. Biol. Chem. 271: 19124–8. doi:10.1074/jbc.271.32.19124. PMID 8702587.
Singh SK, Matsuno K, LaPorte DC, Banaszak LJ (2001). "Crystal structure of Bacillus subtilis isocitrate dehydrogenase at 1.55 A. Insights into the nature of substrate specificity exhibited by Escherichia coli isocitrate dehydrogenase kinase/phosphatase". J. Biol. Chem. 276: 26154–63. doi:10.1074/jbc.M101191200. PMID 11290745.
Jault JM (2001). "The "catalytic" triad of isocitrate dehydrogenase kinase/phosphatase from E. coli and its relationship with that found in eukaryotic protein kinases". Biochemistry. 40: 3047–55. doi:10.1021/bi001713x. PMID 11258918.