Crystallization and preliminary X-ray analysis of an R-2-hydroxypropyl-coenzyme M dehydrogenase.

Nocek B; Clark DD; Ensign SAPeters JW

首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Crystallization and preliminary X-ray analysis of an R-2-hydroxypropyl-coenzyme M dehydrogenase.

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Crystallization and preliminary X-ray analysis of an R-2-hydroxypropyl-coenzyme M dehydrogenase.

机译：结晶和初步的x射线分析一个R-2-hydroxypropyl-coenzyme M脱氢酶。

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The R-2-hydroxypropyl-coenzyme M (2-mercaptoethanesulfonate) dehydrogenase is a key enzyme in the microbial conversion of propylene to the central metabolite acetoacetate. This enzyme is an interesting member of the NAD(P)H-dependent short-chain dehydrogenase/reductase (SDR) family of enzymes, being one of a pair of homologous dehydrogenases that act in concert in a single pathway to convert the R- and S-enantiomers of hydroxypropyl-coenzyme M to the achiral ketopropyl-coenzyme M product. Crystallization trials have revealed that the highest diffraction quality crystals (better than 2.0 A resolution) could be achieved when the reaction substrates were added to the enzyme in a stoichiometric excess prior to crystallization.

机译：R-2-hydroxypropyl-coenzyme米(2-mercaptoethanesulfonate)脱氢酶是一种微生物转化的关键酶丙烯中央代谢物乙酰乙酸盐。这种酶是一个有趣的的成员NAD (P) H-dependent短链脱氢酶/还原酶(SDR)家族的酶,被一对同源脱氢酶之一一致行动的一个途径的R -和S-enantiomers进行转换hydroxypropyl-coenzyme M的非手性的ketopropyl-coenzyme M产品。试验表明,最高衍射2.0质量晶体(比分辨率)当反应底物可以实现被添加到酶在化学计量多余的结晶之前。

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《Acta crystallographica.Section D. Biological crystallography》 |2002年第9期|1470-1473|共4页
作者
Nocek B; Clark DD; Ensign SAPeters JW;
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作者单位

Department of Chemistry and Biochemistry, Montana State University, Bozeman 59717, USA.;

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原文格式 PDF
正文语种英语
中图分类化学;
关键词
Oxidoreductases; Mesna; X-ray analysisDehydrogenasesXanthobacterCrystallization;

机译：氧化还原酶;Mesna;x射线analysisDehydrogenasesXanthobacterCrystallization;

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Crystallization and preliminary X-ray analysis of an R-2-hydroxypropyl-coenzyme M dehydrogenase.

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