Structural and biochemical analyses of YvgN and YtbE from Bacillus   subtilis

doi:10.1002/pro.178

CORC > 北京大学 > 生命科学学院

	Structural and biochemical analyses of YvgN and YtbE from Bacillus subtilis
	Lei, Jian ; Zhou, Yan-Feng ; Li, Lan-Fen ; Su, Xiao-Dong
刊名	蛋白质科学
	2009
关键词	aldo-keto reductase (beta/alpha)(8) TIM barrel fold heteroaromatic aldehyde YtbE/YvgN HUMAN ALDOSE REDUCTASE ALDEHYDE REDUCTASE HUMAN LIVER INHIBITOR MECHANISM SUBSTRATE DEHYDROGENASE PURIFICATION SPECIFICITY COMPLEXES
DOI	10.1002/pro.178
英文摘要	Bacillus subtilis is one of the most studied gram-positive bacteria. In this work, YvgN and YtbE from B. subtilis, assigned as AKR5G1 and AKR5G2 of aldo-keto reductase (AKR) superfamily. AKR catalyzes the NADPH-dependent reduction of aldehyde or aldose substrates to alcohols. YvgN and YtbE were studied by crystallographic and enzymatic analyses. The apo structures of these proteins were determined by molecular replacement, and the structure of holoenzyme YvgN with NADPH was also solved, revealing the conformational changes upon cofactor binding. Our biochemical data suggest both YvgN and YtbE have preferential specificity for derivatives of benzaldehyde, such as nitryl or halogen group substitution at the 2 or 4 positions. These proteins also showed broad catalytic activity on many standard substrates of AKR, such as glyoxal, dihydroxyacetone, and DL-glyceraldehyde, suggesting a possible role in bacterial detoxification.; Biochemistry & Molecular Biology; SCI(E); PubMed; 9; ARTICLE; 8; 1792-1800; 18
语种	英语
内容类型	期刊论文
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/162572]
专题	生命科学学院
推荐引用方式 GB/T 7714	Lei, Jian,Zhou, Yan-Feng,Li, Lan-Fen,et al. Structural and biochemical analyses of YvgN and YtbE from Bacillus subtilis[J]. 蛋白质科学,2009.
APA	Lei, Jian,Zhou, Yan-Feng,Li, Lan-Fen,&Su, Xiao-Dong.(2009).Structural and biochemical analyses of YvgN and YtbE from Bacillus subtilis.蛋白质科学.
MLA	Lei, Jian,et al."Structural and biochemical analyses of YvgN and YtbE from Bacillus subtilis".蛋白质科学 (2009).