Affiliation:
1. School of Pharmaceutical Science and Technology, Health Sciences Platform, Tianjin University, Tianjin 300072, China
Abstract
AbstractCYP20A1 is a well-conserved member of the human cytochrome P450 enzyme family for which no endogenous or xenobiotic substrate is known. We have recently shown that this enzyme has moderate activity towards two proluciferin probe substrates. In order to facilitate the search for physiological substrates we have tested nine additional proluciferins in this study and identified three such probe substrates that give much higher product yields. Using one of these probes, we demonstrate inhibition of CYP20A1 activity by 1-benzylimidazole, ketoconazole and letrozole. Finally, we show that the combination of two common single nucleotide polymorphisms (SNPs) ofCYP20A1leads to an enzyme (CYP20A1Leu97Phe346) with reduced activity.
Subject
Clinical Biochemistry,Molecular Biology,Biochemistry
Cited by
12 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献