Synthetic chemistry and chemical precedents for understanding the structure and function of acetyl coenzyme A synthase.

Synthetic chemistry and chemical precedents for understanding the structure and function of acetyl coenzyme A synthase.
复制标题

了解乙酰辅酶 A 合酶结构和功能的合成化学和化学先例。

DOI:
10.1007/s00775-004-0567-7
复制
发表时间:
2004
期刊:
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry
影响因子:
--
通讯作者:
Riordan,CharlesG
Riordan,CharlesG
中科院分区:
--
文献类型:
--
作者:
Riordan,CharlesG

文献摘要

相似文献

乙酰辅酶A合成酶(ACS)存在于产乙酸菌和产甲烷菌中,负责乙酸乙酯的合成和分解。甲基钴(III)丙氨酸、CO和辅酶A在活性中心A-簇上组装/分解的机制涉及许多生物上前所未有的中间体。在过去的两年中,两种蛋白质的晶体结构显著提高了人们对活性中心A-簇结构的理解,这些结构负责催化作用。这些结构报告引发了一些关于活性酶的金属离子组成、光谱鉴定状态的结构(S)和催化机理细节的重要问题。这篇评论在现有合成和化学先例研究的框架内解决了这些问题,旨在发展合理的结构-功能相关性,并为未来的研究提出了结构和活性目标。
Acetyl coenzyme A synthase (ACS), found in acetogenic and methanogenic organisms, is responsible for the synthesis and breakdown of acetate. The mechanism by which methylcob(III)alamin, CO and coenzyme A are assembled/disassembled at the active-site A-cluster involves a number of biologically unprecedented intermediates. In the past two years, two protein crystal structures have significantly enhanced the understanding of the structure of the active-site A-cluster, responsible for catalysis. The structure reports spawned a number of important questions regarding the metal ion constitution of the active enzyme, the structure(s) of the spectroscopically identified states and the details of the catalytic mechanism. ThisCommentaryaddresses these issues in the framework of existing synthetic and chemical precedent studies aimed at developing rational structure–function correlations and presents structural and reactivity targets for future studies.