Suppr超能文献

吡哆醛酶:机制的多样性与一致性

Pyridoxal enzymes: mechanistic diversity and uniformity.

作者信息

Hayashi H

机构信息

Department of Biochemistry, Osaka Medical College.

出版信息

J Biochem. 1995 Sep;118(3):463-73. doi: 10.1093/oxfordjournals.jbchem.a124931.

Abstract

Pyridoxal 5'-phosphate (PLP) acts as the coenzyme in a vast number of reactions in amino acid metabolism. The study of PLP enzymes is one of the most fascinating frontiers in enzymology, and now the mechanism s of several types of PLP enzymes are being discussed at the atomic level based on crystallographic, spectroscopic, and site-directed mutagenesis studies. In this review, I summarize the important findings, including those provided by classical studies, on the reaction mechanisms of several PLP enzymes, with the intention of discussing the chemically and thermodynamically consistent principle of the catalytic action of PLP enzymes common to all the enzymes of this group, and the uniqueness of individual enzymes that endows them substrate and reaction specificity.

摘要

磷酸吡哆醛(PLP)在氨基酸代谢的大量反应中作为辅酶发挥作用。对PLP酶的研究是酶学中最引人入胜的前沿领域之一,目前基于晶体学、光谱学和定点诱变研究,正在原子水平上讨论几种类型PLP酶的作用机制。在这篇综述中,我总结了包括经典研究在内的关于几种PLP酶反应机制的重要发现,旨在讨论该类所有酶共有的PLP酶催化作用在化学和热力学上一致的原理,以及赋予它们底物和反应特异性的个别酶的独特性。

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验