title: Reversible conversion of tyrosine hydroxylase to an inactive form by antipain.
abstract: Tyrosine hydroxylase, the rate-limiting enzyme in the biosynthesis of catecholamines, was reversibly inactivated by incubation with antipain, which is known as a microbial protease inhibitor. The inactivation was a time-dependent reaction and it was prominent when the enzyme was assayed at a neutral pH but not when assayed at an acidic pH. The inactivated enzyme was markedly activated by cyclic AMP-dependent protein kinase. Other microbial protease inhibitors such as leupeptin, chymostatin, and pepstatin did not induce such as inactivation of the enzyme.
mesh_terms: D000818:Animals; D000976:Antipain / Q000494:pharmacology*; D003342:Corpus Striatum / Q000201:enzymology; D004789:Enzyme Activation; D007700:Kinetics; D009842:Oligopeptides / Q000494:pharmacology*; D011494:Protein Kinases / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D014446:Tyrosine 3-Monooxygenase / Q000037:antagonists & inhibitors / Q000378:metabolism*
chemical_list: D009842:Oligopeptides; D000976:Antipain; D014446:Tyrosine 3-Monooxygenase; D011494:Protein Kinases