Biology:Isocitrate dehydrogenase (NADP+) kinase
| [isocitrate dehydrogenase (NADP+)] kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.7.11.5 | ||||||||
| CAS number | 83682-93-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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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+)] [math]\displaystyle{ \rightleftharpoons }[/math] 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).
Other names
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.
References
- "The reversible phosphorylation of isocitrate dehydrogenase of Salmonella typhimurium". Arch. Biochem. Biophys. 218 (1): 59–67. 1982. doi:10.1016/0003-9861(82)90321-6. PMID 6756316.
- "Isocitrate dehydrogenase kinase/phosphatase. Kinetic characteristics of the wild-type and two mutant proteins". J. Biol. Chem. 271 (32): 19124–8. 1996. doi:10.1074/jbc.271.32.19124. PMID 8702587.
- "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 (28): 26154–63. 2001. doi:10.1074/jbc.M101191200. PMID 11290745.
- Jault JM; Cortay, JC; Blanchet, C; Laporte, DC; Di Pietro, A; Cozzone, AJ; 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 (10): 3047–55. doi:10.1021/bi001713x. PMID 11258918.
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