The enzyme is activated by AMP and is specific for its substrate. Phosphorylates and activates EC 2.7.11.31, [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase, that has been inactivated by EC 3.1.3.16, protein-serine/threonine phosphatase.
History
EC 2.7.11.3 created 1984 as EC 2.7.1.110, transferred 2005 to EC 2.7.11.3
Characterization and regulation of reductase kinase, a protein kinase that modulates the enzymic activity of 3-hydroxy-3-methylglutaryl-coenzyme A reductase.
Reversible modulation of the activities of both liver microsomal hydroxymethylglutaryl coenzyme A reductase and its inactivating enzyme. Evidence for regulation by phosphorylation-dephosphorylation.
Phosphorylation of hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase and modulation of its enzymic activity by calcium-activated and phospholipid-dependent protein kinase.
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.