Identification and Characterization of a Novel Member of the Radical AdoMet Enzyme Superfamily and Implications for the Biosynthesis of the Hmd Hydrogenase Active Site Cofactor

被引：36

作者：

McGlynn, Shawn E. ^{[1
,2
]}

Boyd, Eric S. ^{[1
,2
]}

Shepard, Eric M. ^{[1
,2
]}

Lange, Rachel K. ^{[1
,2
]}

Gerlach, Robin ^{[3
]}

Broderick, Joan B. ^{[1
,2
]}

Peters, John W. ^{[1
,2
]}

机构：

[1] Montana State Univ, Dept Chem & Biochem, Bozeman, MT 59717 USA

[2] Montana State Univ, Astrobiol Biogeocatalysis Res Ctr, Bozeman, MT 59717 USA

[3] Montana State Univ, Dept Chem & Biol Engn, Bozeman, MT 59717 USA

来源：

JOURNAL OF BACTERIOLOGY | 2010年 / 192卷 / 02期

关键词：

DNA-REPAIR ENZYME; CRYSTAL-STRUCTURE; FEFE HYDROGENASE; H-CLUSTER; IRON; PROTEIN; SAM; CLASSIFICATION; VISUALIZATION; MATURATION;

D O I：

10.1128/JB.01125-09

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The genetic context, phylogeny, and biochemistry of a gene flanking the H-2-forming methylene-H-4-methanopterin dehydrogenase gene (hmdA), here designated hmdB, indicate that it is a new member of the radical S-adenosylmethionine enzyme superfamily. In contrast to the characteristic CX3CX2C or CX2CX4C motif defining this family, HmdB contains a unique CX5CX2C motif.

引用

页码：595 / 598

页数：4

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