Abstract

Transaminases (aminotransferases) are stereospecific enzymes catalyzing the reversible amino group transfer from various substrates. Transaminases are key enzymes in amino acid metabolism in all organisms, and they show promise for fine organic synthesis. Among a diversity of transaminases, as-yet poorly characterized pyridoxal 5′-phosphate-dependent fold type IV transaminases have attracted great interest. This transaminase family shows specificity for both D- and L-amino acids and (R)-amines. The crystal structure of thermally stable fold type IV branched-chain amino acid transaminase from the archaeon Thermoproteus uzoniensis in complex with the non-natural substrate L-norvaline was established. The mechanism of substrate binding is considered. The key amino acids involved in the substrate binding are described.

中文翻译：

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乌兹热变形杆菌与L-去甲缬氨酸配合物的支链氨基酸转氨酶的三维结构

摘要

转氨酶（氨基转移酶）是催化从各种底物中可逆氨基转移的立体特异性酶。转氨酶是所有生物体氨基酸代谢中的关键酶，它们有望实现精细的有机合成。在多种转氨酶中，迄今尚未充分表征的吡pyr醛5'-磷酸盐依赖性折叠IV型转氨酶引起了极大的兴趣。该转氨酶家族对D-和L-氨基酸以及（R）-胺均显示特异性。古细菌Thermoproteus uzoniensis的热稳定折叠IV型支链氨基酸转氨酶的晶体结构与非天然底物复合的L-正缬氨酸被建立。考虑底物结合的机理。描述了底物结合中涉及的关键氨基酸。