The methylthiolation reaction mediated by the Radical-SAM enzymes

被引：22

作者：

Atta, Mohamed ^{[1
]}

Arragain, Simon ^{[1
]}

Fontecave, Marc ^{[1
,4
]}

Mulliez, Etienne ^{[1
]}

Hunt, John F. ^{[2
,3
]}

Luff, Jon D. ^{[2
,3
]}

Forouhar, Farhad ^{[2
,3
]}

机构：

[1] CEA Grenoble, UMR CEA CNRS UJF 5249, Inst Rech Technol & Sci Vivant IRTSV LCBM, F-38054 Grenoble 09, France

[2] Columbia Univ, Dept Biol Sci, New York, NY 10027 USA

[3] Columbia Univ, NE Struct Genom Consortium, New York, NY 10027 USA

[4] Coll France, F-75005 Paris, France

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS | 2012年 / 1824卷 / 11期

关键词：

Iron-sulfur cluster; Radical-SAM; tRNA; Methylthiotransferase; Ribosomal S12 protein; RIBOSOMAL-PROTEIN S12; CRYSTAL-STRUCTURE; TRANSFER-RNA; ADENOSYLMETHIONINE; MIAB; IDENTIFICATION; METHYLATION; THIOLATION; SEQUENCES; BINDING;

D O I：

10.1016/j.bbapap.2011.11.007

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

Over the past 10 years. considerable progress has been made in our understanding of the mechanistic enzymology of the Radical-SAM enzymes. It is now clear that these enzymes appear to be involved in a remarkably wide range of chemically challenging reactions. This review article highlights mechanistic and structural aspects of the methylthiotransferases (MTTases) sub-class of the Radical-SAM enzymes. The mechanism of methylthio insertion, now observed to be performed by three different enzymes is an exciting unsolved problem. This article is part of a Special Issue entitled: Radical SAM enzymes and Radical Enzymology. (C) 2011 Elsevier B.V. All rights reserved.

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收藏

页码：1223 / 1230

页数：8

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