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

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Edwards P,Nelsen JS,Metz JG,Dehesh K

doi

10.1016/s0014-5793(96)01437-8

subject

Has Abstract

pub_date

1997-01-27 00:00:00

pages

62-6

issue

1

eissn

0014-5793

issn

1873-3468

pii

S0014579396014378

journal_volume

402

pub_type

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