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  • 标题:Carbonyl Reductase Activity Exhibited by Pig Testicular 20β-Hydroxysteroid Dehydrogenase
  • 本地全文:下载
  • 作者:Shizuo NAKAJIN ; Fumihiro TAMURA ; Noriko TAKASE
  • 期刊名称:Biological and Pharmaceutical Bulletin
  • 印刷版ISSN:0918-6158
  • 电子版ISSN:1347-5215
  • 出版年度:1997
  • 卷号:20
  • 期号:11
  • 页码:1215-1218
  • DOI:10.1248/bpb.20.1215
  • 出版社:The Pharmaceutical Society of Japan
  • 摘要:The carbonyl reductase activity exhibited by pig testicular 20β-hydroxysteroid dehydrogenase (20β-HSD) was examined using a recombinant enzyme. Kinetic parameters were obtained for 48 carbonyl group-containing substrates, including aromatic aldehydes, aromatic ketones, cycloketones, quinones, aliphatic aldehydes and aliphatic ketones. 20β-HSD showed a high affinity towards quinones, such as 9, 10-phenanthrenequinone, α-naphthoquinone and menadione (Km values of 4, 2 and 5 μM, respectively), and the substrate utilization efficiency (Vmax/Km) of the enzyme against these quinones was very high. Cyclohexanone and 2-methylcyclohexanone were also reduced with a high Vmax/Km value, but not cyclopentanone or 2-methylcyclopentanone. Various aromatic aldehydes and ketones including benzaldehyde- and acetophenone-derivatives were reduced by 20β-HSD. Especially, 4-nitrobenzaldehyde and 4-nitroacetophenone were reduced with high Vmax/Km values in related compounds. The enzyme also reduced the pyridine-derivatives, 2-, 3-, and 4-benzoylpyridine, with the Vmax/Km value for 2-benzoylpyridine being the highest. 20β-HSD reduced aliphatic aldehydes and aliphatic ketones, but was more effective on the former. The correlation between the structure of carbonyl compounds and their substrate Vmax/Km is discussed.
  • 关键词:20β-hydroxysteroid dehydrogenase;testis;pig;carbonyl reductase;kinetics;recombinant enzyme
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