• Source: Dephospho-(reductase kinase) kinase

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}



⇌


{\displaystyle \rightleftharpoons }

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



Beg ZH, Stonik JA, Brewer HB Jr (1979). "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. Bibcode:1979PNAS...76.4375B. doi:10.1073/pnas.76.9.4375. PMC 411577. PMID 291971.
Ingebritsen TS, Lee HS, Parker RA, Gibson DM (1978). "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. doi:10.1016/0006-291X(78)91273-1. PMID 666819.
Beg ZH, Stonik JA, Brewer HB Jr (1985). "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. doi:10.1016/S0021-9258(18)89648-X. PMID 3155737.
Clarke PR, Hardie DG (1990). "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. doi:10.1002/j.1460-2075.1990.tb07420.x. PMC 552270. PMID 2369897.
Sato R, Goldstein JL, Brown MS (1993). "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. Bibcode:1993PNAS...90.9261S. doi:10.1073/pnas.90.20.9261. PMC 47547. PMID 8415689.

Kata Kunci Pencarian:

• MAP kinase kinase kinase
• Reductase kinase
• Extracellular signal-regulated kinases
• CAMK
• Protein kinase A
• Phosphorylase kinase
• Dephospho-(reductase kinase) kinase
• Mitogen-activated protein kinase kinase
• RAF kinase
• AMP-activated protein kinase