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甾体生成细胞色素 P450 酶结构中的多样性和底物特异性。

Diversity and substrate specificity in the structures of steroidogenic cytochrome P450 enzymes.

机构信息

Biometal Science Laboratory, RIKEN SPring Center, Sayo, Hyogo, Japan.

出版信息

Biol Pharm Bull. 2012;35(6):818-23. doi: 10.1248/bpb.35.818.

DOI:10.1248/bpb.35.818
PMID:22687469
Abstract

Mammalian cytochrome P450 (CYP) comprise a large group of enzymes that play many important roles in the biosynthesis of steroid hormones and vitamins. In addition, they participate in the metabolism of drugs and xenobiotics. All known mammalian CYP enzymes are membrane-associated proteins, which complicated their X-ray crystallographic analysis. In recent years, however, significant progress has been made in the X-ray crystallographic analysis of mammalian CYP enzymes involved in the steroid hormone and vitamin D(3) metabolism. The knowledge from three-dimensional structures of mammalian CYP enzymes will benefit drug discovery and development.

摘要

哺乳动物细胞色素 P450(CYP)是一大类酶,在甾体激素和维生素的生物合成中发挥着许多重要作用。此外,它们还参与药物和外源化合物的代谢。所有已知的哺乳动物 CYP 酶都是膜相关蛋白,这使得它们的 X 射线晶体学分析变得复杂。然而,近年来,在参与甾体激素和维生素 D(3)代谢的哺乳动物 CYP 酶的 X 射线晶体学分析方面取得了重大进展。来自哺乳动物 CYP 酶三维结构的知识将有益于药物发现和开发。

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