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Cloning of the fabF gene in an expression vector and in vitro characterization of recombinant fabF and fabB encoded enzymes from Escherichia coli
Author(s) -
Edwards Patricia,
Sabo Nelsen Janet,
Metz James G,
Dehesh Katayoon
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01437-8
Subject(s) - recombinant dna , gene , escherichia coli , microbiology and biotechnology , biology , cloning (programming) , molecular cloning , enzyme , genomic dna , biochemistry , genetics , gene expression , computer science , programming language
Analysis of the β‐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.