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 Lettjournal_title
FEBS lettersauthors
Edwards P,Nelsen JS,Metz JG,Dehesh Kdoi
10.1016/s0014-5793(96)01437-8subject
Has Abstractpub_date
1997-01-27 00:00:00pages
62-6issue
1eissn
0014-5793issn
1873-3468pii
S0014579396014378journal_volume
402pub_type
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