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Updated: Jun 23, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

サイクロヘクサノンモノオキシゲネーゼの結晶構造は,複雑なドメインの動きとスライディングコファクターを示しています

I Ahmad Mirza1, Brahm J Yachnin, Shaozhao Wang

  • 1Department of Biochemistry, McGill University, 3649 Prom Sir William Osler, Bellini Pavilion, Room 466, Montreal, QC, Canada H3G 0B1.

Journal of the American Chemical Society
|April 24, 2009
PubMed
まとめ

サイクロヘクサノンモノオキシゲナーゼ (CHMO) は,ベイヤー-ヴィリガー酸化を触媒化する. 構造分析は,コファクターの位置付けと基板結合に不可欠なドメインシフトとループの動きを明らかにし,この酵素反応のメカニズム的な洞察を提供します.

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