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从碱性应激细菌培养物中纯化的大肠杆菌色氨酸酶的结构

Structure of Escherichia coli tryptophanase purified from an alkaline-stressed bacterial culture.

作者信息

Rety Stephane, Deschamps Patrick, Leulliot Nicolas

机构信息

Laboratoire de Cristallographie et RMN Biologiques, UMR CNRS 8015, Université Paris Descartes, Sorbonne Paris Cité, Faculté de Pharmacie de Paris, Paris, France.

出版信息

Acta Crystallogr F Struct Biol Commun. 2015 Nov;71(Pt 11):1378-83. doi: 10.1107/S2053230X15017549. Epub 2015 Oct 23.

Abstract

Tryptophanase is a bacterial enzyme involved in the degradation of tryptophan to indole, pyruvate and ammonia, which are compounds that are essential for bacterial survival. Tryptophanase is often overexpressed in stressed cultures. Large amounts of endogenous tryptophanase were purified from Escherichia coli BL21 strain overexpressing another recombinant protein. Tryptophanase was crystallized in space group P6522 in the apo form without pyridoxal 5'-phosphate bound in the active site.

摘要

色氨酸酶是一种细菌酶,参与将色氨酸降解为吲哚、丙酮酸和氨,这些化合物是细菌生存所必需的。色氨酸酶在应激培养物中常常过度表达。从过表达另一种重组蛋白的大肠杆菌BL21菌株中纯化出了大量内源性色氨酸酶。色氨酸酶以无辅基形式在空间群P6522中结晶,活性位点未结合磷酸吡哆醛。

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