猪肾氨基酰化酶活性中心及催化机理的研究:一个活性中心模型。

B Szajáni, A Kiss, L Boross
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引用次数: 0

摘要

苯基甲基磺酰氟和烷基化剂(碘乙酸或碘乙酰胺)都不能抑制普氨酸肾氨基酰化酶(E.C. 3.5.1.14)。因此,包括通过丝氨酸或半胱氨酸侧链形成酰基酶的反应机制被排除在外。该酶是一种金属蛋白,可以被ECTA灭活,其中Co2+是Zn2+离子的等效替代品。氨基酰化酶的两个SH基团/亚基对对羟基汞苯甲酸酯表现出不同的反应活性。活性较低的SH基团的修饰可逆地使酶失活。我们认为这个半胱氨酸侧链位于活性中心或其附近。根据我们的结果,我们认为在活性中心和催化机制方面,氨基酰化酶和羧肽酶a非常相似。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Investigation of the active center and catalytic mechanism of porcine kidney aminoacylase: a model of the active center.

Procine kidney aminoacylase (E.C. 3.5.1.14) is inhibited neither by phenylmethylsulfonylfluoride nor by alkylating agents (iodoacetate or iodoacetamide). Therefore reaction mechanisms including the formation of acylenzyme through seryl or cysteinyl side chains are ruled out. The enzyme is a metalloprotein that can be inactivated by ECTA and in which Co2+ is an equivalent substitute for the Zn2+ ion. The two SH groups/subunit of aminoacylase exhibit different reactivites to p-hydroxymercuribenzoate. Modification of the less reactive SH group reversibly inactivates the enzyme. We suggest that this cysteinyl side chain is situated in the active center or in its immediate vicinity. On the basis of our results we suppose a close similarity between aminoacylase and carboxypeptidase A with respect to their active center and catalytic mechanism.

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