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  • Title: Reversible conversion of tyrosine hydroxylase to an inactive form by antipain.
    Author: Okuno S, Fujisawa H.
    Journal: Biochem Biophys Res Commun; 1987 Aug 14; 146(3):1375-81. PubMed ID: 2887168.
    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.
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