Biology:Dephospho-(reductase kinase) kinase
| dephospho-[reductase kinase] kinase | |||||||||
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| Identifiers | |||||||||
| EC number | 2.7.11.3 | ||||||||
| CAS number | 72060-33-4 | ||||||||
| 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 dephospho-[reductase kinase] kinase (EC 2.7.11.3) is an enzyme that catalyzes the chemical reaction
- ATP + dephospho-{[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase} [math]\displaystyle{ \rightleftharpoons }[/math] ADP + {[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase}
Thus, the two substrates of this enzyme are ATP and dephospho-{[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase}, whereas its two products are ADP and {[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase}.
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:dephospho-{[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase} phosphotransferase. Other names in common use include AMP-activated kinase, AMP-activated protein kinase kinase, hydroxymethylglutaryl coenzyme A reductase kinase kinase, hydroxymethylglutaryl coenzyme A reductase kinase kinase, (phosphorylating), reductase kinase, reductase kinase kinase, and STK30.
References
- "Characterization and regulation of reductase kinase, a protein kinase that modulates the enzymic activity of 3-hydroxy-3-methylglutaryl-coenzyme A reductase". Proc. Natl. Acad. Sci. U.S.A. 76 (9): 4375–9. 1979. doi:10.1073/pnas.76.9.4375. PMID 291971. Bibcode: 1979PNAS...76.4375B.
- "Reversible modulation of the activities of both liver microsomal hydroxymethylglutaryl coenzyme A reductase and its inactivating enzyme. Evidence for regulation by phosphorylation-dephosphorylation". Biochem. Biophys. Res. Commun. 81 (4): 1268–77. 1978. doi:10.1016/0006-291X(78)91273-1. PMID 666819.
- "Phosphorylation of hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase and modulation of its enzymic activity by calcium-activated and phospholipid-dependent protein kinase". J. Biol. Chem. 260 (3): 1682–7. 1985. doi:10.1016/S0021-9258(18)89648-X. PMID 3155737.
- "Regulation of HMG-CoA reductase: identification of the site phosphorylated by the AMP-activated protein kinase in vitro and in intact rat liver". EMBO J. 9 (8): 2439–46. 1990. doi:10.1002/j.1460-2075.1990.tb07420.x. PMID 2369897.
- "Replacement of serine-871 of hamster 3-hydroxy-3-methylglutaryl-CoA reductase prevents phosphorylation by AMP-activated kinase and blocks inhibition of sterol synthesis induced by ATP depletion". Proc. Natl. Acad. Sci. U.S.A. 90 (20): 9261–5. 1993. doi:10.1073/pnas.90.20.9261. PMID 8415689. Bibcode: 1993PNAS...90.9261S.
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