Okuno S, Fujisawa H
Biochem Biophys Res Commun. 1987 Aug 14;146(3):1375-81. doi: 10.1016/0006-291x(87)90801-1.
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.
酪氨酸羟化酶是儿茶酚胺生物合成中的限速酶，与抗蛋白酶一起孵育后会被可逆性失活，抗蛋白酶是一种已知的微生物蛋白酶抑制剂。这种失活是一种时间依赖性反应，当在中性pH下测定该酶时很明显，但在酸性pH下测定时则不明显。失活的酶可被环磷酸腺苷依赖性蛋白激酶显著激活。其他微生物蛋白酶抑制剂，如亮抑蛋白酶肽、抑糜蛋白酶素和胃蛋白酶抑制剂，不会诱导该酶发生这种失活。
