Cloning of the fabF gene in an expression vector and in vitro characterization of recombinant fabF and fabB encoded enzymes from Escherichia coli

被引：85

作者：

Edwards, P ^{[1
]}

Nelsen, JS ^{[1
]}

Metz, JG ^{[1
]}

Dehesh, K ^{[1
]}

机构：

[1] CALGENE INC,OILS DIV,DAVIS,CA 95616

来源：

FEBS LETTERS | 1997年 / 402卷 / 01期

关键词：

fabF; fabJ; affinity purification; recombinant enzyme; thermal regulation; beta-ketoacyl-ACP synthase;

D O I：

10.1016/S0014-5793(96)01437-8

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：

Analysis of the beta-ketoacyl-ACP synthase (KAS) encoded by the fabF gene of Escherichia coli has been hampered by a reported instability of the cloned gene. Here we describe biochemical characterization of purified, active protein from the recombinant fabF gene. This enzyme has the properties ascribed to KAS II and not those of a putative KAS IV reported to be encoded by fabJ, a genomic clone with DNA sequence identical to that of fabF, We also characterize active protein from a recombinant fabB gene and suggest that this method may have a general utility for analysis of KAS enzymes.

引用

页码：62 / 66

页数：5

共 23 条

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