STRUCTURE OF PORCINE ALDEHYDE REDUCTASE HOLOENZYME
STRUCTURE OF PORCINE ALDEHYDE REDUCTASE HOLOENZYME
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DOI：
10.1038/nsb0895-687
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发表时间：
1995-08-01
期刊：
影响因子：
--
通讯作者：
FLYNN, TG
中科院分区：
文献类型：
--
作者：
ELKABBANI, O;JUDGE, K;FLYNN, TG
醛还原酶是醛-酮还原酶超家族的成员，催化多种醛依赖于NADPH还原为它们相应的醇。猪醛还原酶-NADPH二元复合物的结构已通过X-射线衍射方法确定，并在2.4埃分辨率下精确到0.20的晶体学R因子。醛还原酶的三级结构与醛糖还原酶的三级结构相似，由α/β-桶组成，活性位点位于桶链的羧基末端。与醛糖还原酶不同，醛还原酶中His 113的咪唑环的N-2通过氢键与NADPH的烟酰胺环的酰胺基相互作用。
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.