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HemN 样自由基 S-腺苷甲硫氨酸酶催化反应的最新进展。

Recent advances in HemN-like radical S-adenosyl-l-methionine enzyme-catalyzed reactions.

机构信息

State Key Laboratory of Bio-organic and Natural Products Chemistry, Center for Excellence in Molecular Synthesis, Shanghai Institute of Organic Chemistry, University of Chinese Academy of Sciences, Chinese Academy of Sciences, 345 Lingling Road, Shanghai 200032, China.

出版信息

Nat Prod Rep. 2020 Jan 1;37(1):17-28. doi: 10.1039/c9np00032a. Epub 2019 Jul 10.

Abstract

Covering: 2012 to 2019HemN-like radical S-adenosyl-l-methionine (SAM) enzymes have been recently disclosed to catalyze diverse chemically challenging reactions from primary to secondary metabolic pathways. In this highlight, we summarize the reaction examples catalyzed by HemN-like enzymes to date and the enzymatic mechanisms reported. From the recent mechanistic investigations, we reason that there is a shared initiating mechanism wherein a characteristic SAM methylene radical is proposed to abstract a hydrogen atom from an sp carbon or add onto an sp carbon center although variations occur thereafter from reaction to reaction, as well as providing a brief insight into some future prospects.

摘要

涵盖

2012 年至 2019 年

最近发现 HemN 样自由基 S-腺苷甲硫氨酸(SAM)酶能够催化从初级到次级代谢途径的各种具有挑战性的化学反应。在这篇重点介绍中,我们总结了迄今为止由 HemN 样酶催化的反应实例和报道的酶促机制。从最近的机制研究来看,我们认为存在一个共同的起始机制,其中一个特征性的 SAM 亚甲基自由基被提出从 sp 碳或添加到 sp 碳中心上提取一个氢原子,尽管此后从一个反应到另一个反应会发生变化,同时也对一些未来的前景提供了简要的见解。

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