Structural and biochemical characterization of FabK from Thermotoga maritima

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• 作者：Byung Hak Ha^a ; ¹ ; Sang Chul Shin^a ; ^c ; ¹ ; Jin Ho Moon^a ; Gyochang Keum^b ; Chan-Wha Kim^c ; Eunice EunKyeong Kim^a ; ^{eunice@kist.re.kr}
• 关键词：FabK ; Enoyl-acyl carrier protein (ACP) reductase ; Crystal structure ; Biochemical characterization
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2017
• 出版时间：22 January 2017
• 年：2017
• 卷：482
• 期：4
• 页码：968-974
• 全文大小：1754 K
• 卷排序：482

文摘

Crystal structures of TM0800 with and without FMN are determined. It consists of two domains: the N-terminal TIM barrel and a lid domain. FMN binds at the interface with two methionine packing on the isoalloxazine ring. Mutagenesis studies show Met276 and Ser280 are important in the enzymatic activity. Structural and biochemical studies show TM0800 is FabK, enoyl-ACP-reductase II.