BENZO(A)PYRENE HYDROXYLASE-ACTIVITY IN YEAST IS MEDIATED BY P450 OTHER THAN STEROL 14-ALPHA-DEMETHYLASE

被引：21

作者：

KELLY, SL ^{[1
]}

LAMB, DC ^{[1
]}

BALDWIN, BC ^{[1
]}

KELLY, DE ^{[1
]}

机构：

[1] ZENECA AGROCHEM,JEALOTTS HILL RES STN,BRACKNELL,BERKS,ENGLAND

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1993年 / 197卷 / 02期

关键词：

D O I：

10.1006/bbrc.1993.2497

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：

Benzo(a)pyrene hydroxylation has been observed in Saccharomyces cerevisiae and the role of sterol 14α-demethylase (CYP51A1) in this activity has been examined by using a strain which contains a gene disruption of CYP51A1. This strain still contained P450 protein(s) with a Soret absorption maximum at 448nm in reduced carbon monoxide difference spectra of the microsomal fraction. On addition of benzo(a)pyrene to this microsomal extract a typical Type I substrate-binding spectrum was obtained and was also observed for the isogenic sister strain containing no CYP51A1 gene disruption. Microsomal extracts of both strains had equivalent activity in the aryl hydrocarbon hydroxylase assay. These results indicate a yeast benzo(a)pyrene hydroxylase activity distinct from sterol 14α-demethylase P450. © 1993 Academic Press, Inc.

引用

页码：428 / 432

页数：5

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