ANALYSIS OF THE CATALYTIC SPECIFICITY OF CYTOCHROME-P450 ENZYMES THROUGH SITE-DIRECTED MUTAGENESIS

被引：37

作者：

JOHNSON, EF ^{[1
]}

KRONBACH, T ^{[1
]}

HSU, MH ^{[1
]}

机构：

[1] GODECKE AG, DEPT DRUG METAB, W-7800 FREIBURG, GERMANY

来源：

FASEB JOURNAL | 1992年 / 6卷 / 02期

关键词：

ENZYME ENGINEERING; SITE-DIRECTED MUTAGENESIS; CYTOCHROME-P450; PROGESTERONE; 21-HYDROXYLATION;

D O I：

10.1096/fasebj.6.2.1537459

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The way in which structural diversity encodes the capacity of individual P450 enzymes to metabolize multiple, structurally distinct substrates remains largely unknown. The tools of molecular biology provide a means of identifying amino acid residues among closely related P450s that are determinants of their distinct catalytic properties. Work in our laboratory has identified two substrate specificity-determining segments of the amino acid sequences of subfamily 2C P450s. A pattern has emerged from this work, and that of others, which suggests a model for the structural basis of P450 catalytic diversity.

引用

页码：700 / 705

页数：6

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