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首页> 外文期刊>Biochemistry >Structure of a Clostridium botulinum C143S thiaminase I/thiamin complex reveals active site architecture
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Structure of a Clostridium botulinum C143S thiaminase I/thiamin complex reveals active site architecture

机译：肉毒梭菌C143S硫胺酶​​I /硫胺复合物的结构揭示了活性位点结构

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摘要

Thiaminases are responsible for the degradation of thiamin and its metabolites. Two classes of thiaminases have been identified based on their three-dimensional structures and their requirements for a nucleophilic second substrate. Although the reactions of several thiaminases have been characterized, the physiological role of thiamin degradation is not fully understood. We have determined the three-dimensional X-ray structure of an inactive C143S mutant of Clostridium botulinum (Cb) thiaminase I with bound thiamin at 2.2 ? resolution. The C143S/thiamin complex provides atomic level details of the orientation of thiamin upon binding to Cb-thiaminase I and the identity of active site residues involved in substrate binding and catalysis. The specific roles of active site residues were probed by using site directed mutagenesis and kinetic analyses, leading to a detailed mechanism for Cb-thiaminase I. The structure of Cb-thiaminase I is also compared to the functionally similar but structurally distinct thiaminase II.
机译：硫胺素负责硫胺素及其代谢产物的降解。基于它们的三维结构和对亲核第二底物的要求，已鉴定出两类硫胺素酶。尽管已表征了几种硫胺素酶的反应，但硫胺素降解的生理作用尚未得到充分了解。我们已经确定了肉毒梭菌（Cb）硫胺素酶I与结合的硫胺素在2.2℃下失活的C143S突变体的三维X射线结构。解析度。 C143S /硫胺素复合物提供了硫胺素与Cb-硫胺素I结合后的原子级详细信息以及参与底物结合和催化的活性位点残基的身份。通过使用定点诱变和动力学分析探测了活性位点残基的特​​定作用，从而得出了Cb-硫胺素I的详细机理。还将Cb-硫胺素I的结构与功能相似但结构不同的硫胺素II进行了比较。

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