STRUCTURE OF PORCINE ALDEHYDE REDUCTASE HOLOENZYME

被引:73
作者
ELKABBANI, O
JUDGE, K
GINELL, SL
MYLES, DAA
DELUCAS, LJ
FLYNN, TG
机构
[1] BROOKHAVEN NATL LAB,NATL SYNCHROTRON LIGHT SOURCE DEPT,ARGONNE NATL LAB,CTR STRUCT BIOL,UPTON,NY 11973
[2] UNIV KEELE,DEPT PHYS,KEELE ST5 5BG,STAFFS,ENGLAND
[3] QUEENS UNIV,DEPT BIOCHEM,KINGSTON,ON K7L 3N6,CANADA
来源
NATURE STRUCTURAL BIOLOGY | 1995年 / 2卷 / 08期
关键词
D O I
10.1038/nsb0895-687
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Aldehyde reductase, a member of the aldo-keto reductase superfamily, catalyzes the NADPH-dependent reduction of a variety of aldehydes to their corresponding alcohols. The structure of porcine aldehyde reductase-NADPH binary complex has been determined by X-ray diffraction methods and refined to a crystallographic R-factor of 0.20 at 2.4 Angstrom resolution. The tertiary structure of aldehyde reductase is similar to that of aldose reductase and consists of an alpha/beta-barrel with the active site located at the carboxy terminus of the strands of the barrel, Unlike aldose reductase, the N epsilon 2 of the imidazole ring of His 113 in aldehyde reductase interacts, through a hydrogen bond, with the amide group of the nicotinamide ring of NADPH.
引用
收藏
页码:687 / 692
页数:6
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