From Suicide Enzyme to Catalyst: The Iron-Dependent Sulfide Transfer in Methanococcus jannaschii Thiamin Thiazole Biosynthesis

被引：30

作者：

Eser, Bekir E. ^{[3
]}

Zhang, Xuan ^{[2
]}

Chanani, Prem K. ^{[1
]}

Begley, Tadhg P. ^{[1
]}

Ealick, Steven E. ^{[2
]}

机构：

[1] Texas A&M Univ, Dept Chem, College Stn, TX 77842 USA

[2] Cornell Univ, Dept Chem & Chem Biol, Ithaca, NY 14853 USA

[3] Zirve Univ, Emine Bahaeddin Nakiboglu Sch Med, Dept Med Biochem, TR-27260 Gaziantep, Turkey

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2016年 / 138卷 / 11期

关键词：

RNA WOBBLE POSITIONS; ACTIVE-SITES; SULFUR-RELAY; MYCOBACTERIUM-TUBERCULOSIS; SACCHAROMYCES-CEREVISIAE; MECHANISTIC INSIGHTS; ACTIVATION; CYSTEINE; PATHWAY; 2-THIOURIDINE;

D O I：

10.1021/jacs.6b00445

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Bacteria and yeast utilize different strategies for sulfur incorporation in the biosynthesis of the thiamin thiazole. Bacteria use thiocarboxylated proteins. In contrast, Saccharomyces cerevisiae thiazole synthase (THI4p) uses an active site cysteine as the sulfide source and is inactivated after a single turnover. Here, we demonstrate that the Thi4 ortholog from Methanococcus jannaschii uses exogenous sulfide and is catalytic. Structural and biochemical studies on this enzyme elucidate the mechanistic details of the sulfide transfer reactions.

引用

页码：3639 / 3642

页数：4