CYP86A1 from Arabidopsis thaliana encodes a cytochrome P450-dependent fatty acid omega-hydroxylase

被引:115
作者
Benveniste, I [1 ]
Tijet, N [1 ]
Adas, F [1 ]
Philipps, G [1 ]
Salaün, JP [1 ]
Durst, F [1 ]
机构
[1] CNRS, Inst Biol Mol Plantes, Dept Enzymol Cellulaire & Mol, F-67083 Strasbourg, France
关键词
fatty acid; hydroxylation; omega-hydroxylase; specificity; CYP4; CYP52; CYP102; higher plant; cutin; defense;
D O I
10.1006/bbrc.1998.8156
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 A. thaliana EST database was screened using consensus motifs derived from P450 families CYP52 and CYP4 catalyzing the omega-hydroxylation of fatty acids and alkanes in Candida and in mammals. One EST cDNA fragment was detected in this way and the corresponding full-length cDNA was cloned from a cDNA library of A. thaliana. This cDNA coded the first member of a new plant P450 family and was termed CYP86A1. The deduced peptide sequence showed highest homology with P450s from families 4 and 52. To confirm the catalytic function, CYP86A1 was expressed in a yeast overexpressing its own NADPH-P450 reductase. Efficient expression was evidenced by spectrophotometry, SDS-PAGE and catalytic activity. CYP86A1 was found to catalyze the omega-hydroxylation of saturated and unsaturated fatty acids with chain lengths from C12 to C18 but not of hexadecane. Genomic organization analyzed by Southern blot suggested a single gene encoding CYP86A1 in A. thaliana. (C) 1998 Academic Press.
引用
收藏
页码:688 / 693
页数:6
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