Pyruvate-containing enzymes
Pyruvate-containing enzymes
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含丙酮酸的酶
DOI：
10.1016/0968-0004(77)90441-8
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发表时间：
1977
影响因子：
13.8
通讯作者：
E. Snell
中科院分区：
文献类型：
--
作者：
E. Snell
氨基酸在代谢过程中发生的大多数转化是由酶催化的，而这些酶被羰基试剂抑制。这种敏感性最常见的原因是催化中心存在s -磷酸吡哆醛，人们对这种辅酶如何协助催化这些反应有很多了解（回顾，见[1]）。事实上，由吡哆醇- p酶催化的反应如此之多，以至于直到最近羰基试剂（如羟胺、各种肼、CN-等）对酶活性的抑制才经常被认为是吡哆醇- p在该反应中起作用的证据。因此，当丙酮酸首次被报道为部分纯化的脯氨酸还原酶制剂（由Hodgins和Abeles制作）和细菌组氨酸脱羧酶（由Riley和Snell制作）中共价结合的催化必需组分时，这是一个非常令人惊讶的发现。自这些研究以来，已经发现并列出了几种含有丙酮酸、a-酮丁酸或相关结构作为共价结合假基的酶
Most of the transformations that amino acids undergo during metabolism are catalyzed by enzymes that are inhibited by carbonyl group reagents. This sensitivity most frequently results from the presence of pyridoxal S-phosphate at the catalytic center, and a great deal is known about how this coenzyme assists in catalysis of these reactions (for a review, see [l]). Indeed, so numerous are the reactions catalyzed by pyridoxal-P enzymes that until recently inhibition of an enzyme activity by carbonyl group reagents (eg hydroxylamines, various hydrazines, CN-, etc.) was frequently accepted as evidence for a role of pyridoxal-P in that reaction. It came as a distinct surprise, therefore, when pyruvate was first reported as a covalently-bound, catalytically essential component of partially purified preparations of proline reductase by Hodgins and Abeles [2], and of homogeneous preparations of a bacterial histidine decarboxylase by Riley and Snell [3]. Since these studies, several additional enzymes that contain pyruvate, a-ketobutyrate or related structures as covalently bound prosthetic groups have been discovered and are listed