Biosynthesis of F0, Precursor of the F420 Cofactor, Requires a Unique Two Radical-SAM Domain Enzyme and Tyrosine as Substrate

被引：63

作者：

Decamps, Laure ^{[2
,3
]}

Philmus, Benjamin ^{[1
]}

Benjdia, Alhosna ^{[4
]}

White, Robert ^{[5
]}

Begley, Tadhg P. ^{[1
]}

Berteau, Olivier ^{[2
,3
]}

机构：

[1] Texas A&M Univ, Dept Chem, College Stn, TX 77843 USA

[2] INRA, UMR Micalis 1319, F-78350 Jouy En Josas, France

[3] AgroParisTech, UMR Micalis, F-78350 Jouy En Josas, France

[4] Max Planck Inst Med Res, Dept Biomol Mech, D-69120 Heidelberg, Germany

[5] Virginia Polytech Inst & State Univ, Dept Biochem, Blacksburg, VA 24061 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2012年 / 134卷 / 44期

基金：

美国国家科学基金会;

关键词：

SULFATASE-MATURATING ENZYMES; COENZYME F-420; MYCOBACTERIUM-TUBERCULOSIS; ESCHERICHIA-COLI; IDENTIFICATION; 7,8-DIDEMETHYL-8-HYDROXY-5-DEAZARIBOFLAVIN; SUPERFAMILY; RIBOFLAVIN; MOAA; NO;

D O I：

10.1021/ja307762b

中图分类号：

O6 [化学];

学科分类号：

070301 [无机化学];

摘要：

Cofactors play key roles in metabolic pathways. Among them F-420 has proved to be a very attractive target for the selective inhibition of archaea and actinobacteria. Its biosynthesis, in a unique manner, involves a key enzyme, F-0-synthase. This enzyme is a large monomer in actinobacteria, while it is constituted of two subunits in archaea and cyanobacteria. We report here the purification of both types of F-0-synthase and their in vitro activities. Our study allows us to establish that F-0-synthase, from both types, uses 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione and tyrosine as substrates but not 4-hydroxylphenylpyruvate as previously suggested. Furthermore, our data support the fact that F-0-synthase generates two 5'-deoxyadenosyl radicals for catalysis which is unprecedented in reaction catalyzed by radical SAM enzymes.

引用

页码：18173 / 18176

页数：4

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