S-Adenosylmethionine-dependent radical-based modification of biological macromolecules

被引：38

作者：

Atta, Mohamed ^{[1
]}

Mulliez, Etienne ^{[1
]}

Arragain, Simon ^{[1
]}

Forouhar, Farhad ^{[2
,3
]}

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

Fontecave, Marc ^{[1
,4
]}

机构：

[1] CEA Grenoble, IRTSV LCBM, UMR CEA CNRS UJF 5249, 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：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2010年 / 20卷 / 06期

关键词：

PYRUVATE FORMATE-LYASE; ANAEROBIC RIBONUCLEOTIDE REDUCTASE; SULFATASE-MATURATING ENZYME; RIBOSOMAL-PROTEIN S12; CRYSTAL-STRUCTURE; TRANSFER-RNA; ESCHERICHIA-COLI; STRUCTURAL BASIS; SAM SUPERFAMILY; 4FE-4S CLUSTERS;

D O I：

10.1016/j.sbi.2010.09.009

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Proteins and RNA molecules enjoy a variety of chemically complex post-translational and post-transcriptional modifications. The chemistry at work in these reactions, which was considered to be exclusively ionic in nature has recently been shown to depend on radical mechanisms in some cases. The overwhelming majority of these radical-based reactions are catalyzed by 'Radical-SAM' enzymes. This review article highlights mechanistic and structural aspects of this class of reactions and indicates important research directions to be addressed.

引用

页码：684 / 692

页数：9

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