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首页> 外文期刊>Biochemistry >Kinetic Analysis of the Bisubstrate Cysteine Desulfurase SufS from Bacillus subtilis
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Kinetic Analysis of the Bisubstrate Cysteine Desulfurase SufS from Bacillus subtilis

机译：枯草芽孢杆菌双底物半胱氨酸脱硫酶SufS的动力学分析

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Cysteine is the major sulfur donor for thio cofactors in bacterial and eukaryotic systems. The firstnstep in sulfur mobilization involves a PLP-dependent enzymatic mechanism. During catalysis, free cysteine isnconverted into alanine with the concomitant formation of a persulfide bondwith the catalytic cysteine residue, thusnforming a covalent enzyme intermediate. Cysteine desulfurases in their persulfurated forms serve as donors at thenintersection of various cellular sulfur-requiring pathways.MostGram-positive bacteria, including Bacillus subtilis,ncontain a cysteine desulfurase gene sufS located adjacent to the gene encoding the proposed Fe-S cluster scaffoldnSufU. In this work, we identified the participation of SufU as a substrate in the SufS catalytic mechanism.nDevelopment of a sensitive method for detection of alanine formed in the SufS reaction enabled the identificationnof its associated mechanistic features. Steady-state kinetic analysis of alanine formation provided evidence of andouble-displacement mechanism (ping-pong) of the cysteine:SufU sulfurtransferase reaction catalyzed by SufS.nResults from site-directed mutagenesis of the catalytic cysteine (SufSC361A) and iodoacetamide alkylation of SufUnsupport the occurrence of persulfide sulfur transfer steps in the mechanism of SufS
机译：半胱氨酸是细菌和真核生物系统中硫辅因子的主要硫供体。硫磺动员的第一步涉及PLP依赖的酶促机制。在催化过程中，游离半胱氨酸转化为丙氨酸，并与催化半胱氨酸残基同时形成过硫键，从而形成共价酶中间体。半胱氨酸脱硫酶以过硫酸盐的形式在各​​种细胞需要硫的途径的交汇处充当供体。包括枯草芽孢杆菌在内的大多数革兰氏阳性细菌都含有一个半胱氨酸脱硫酶基因sufS，它位于编码拟议的Fe-S簇骨架scufoldnSufU的基因附近。在这项工作中，我们确定了SufU作为SufS催化机理的底物。n检测SufS反应中形成的丙氨酸的灵敏方法的开发使人们能够鉴定其相关的机理。丙氨酸形成的稳态动力学分析提供了SufS催化的半胱氨酸：SufU硫转移酶双置换机制（乒乓球）的证据.n催化半胱氨酸（SufSC361A）的定点诱变和SufUn的碘乙酰胺烷基化的结果SufS机理中过硫化物硫转移步骤的发生

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