文章基本信息

标题：Enzymatic Properties of a Member (AKR1C19) of the Aldo-Keto Reductase Family
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作者：Shuhei Ishikura ; Kenji Horie ; Masaharu Sanai 等
期刊名称：Biological and Pharmaceutical Bulletin
印刷版ISSN：0918-6158
电子版ISSN：1347-5215
出版年度：2005
卷号：28
期号：6
页码：1075-1078
DOI：10.1248/bpb.28.1075
出版社：The Pharmaceutical Society of Japan
摘要：A member (AKR1C19) of the aldo-keto reductase (AKR) superfamily, found by mouse genomic analysis, was shown to be highly expressed in the liver and gastrointestinal tract, but its function remains unknown. In this study, the recombinant AKR1C19 was expressed and purified to homogeneity. The enzyme was a 36-kDa monomer, and reduced α-dicarbonyl compounds such as camphorquinone and isatin using both NADH and NADPH as the coenzymes. Although apparent kinetic constants for the two coenzymes were similar, the NADPH-linked activity was potently inhibited by submillimolar concentrations of NAD⁺, but the inhibition of the NADH-linked activity was not significant, suggesting that the enzyme exhibits the NADH-linked reductase activity in vivo . AKR1C19 slowly oxidized 3-hydroxyhexobarbital, S -indan-1-ol and cis -benzene dihydrodiol, but was inactive towards steroids, prostaglandins, monosaccharides, and other xenobiotic alcohols. In addition, the enzyme was inhibited only by dicumarol, lithocholic acid and genistein of various compounds tested. Thus, AKR1C19 possesses properties distinct from other members of the AKR superfamily, and may function as a reductase for endogenous isatin and xenobiotic α-dicarbonyl compounds in the liver and gastrointestinal tract.
关键词：aldo-keto reductase superfamily;AKR1C19;dual coenzyme specificity;isatin;3-hydroxyhexobarbital dehydrogenase