In:
Journal of Bacteriology, American Society for Microbiology, Vol. 180, No. 5 ( 1998-03), p. 1338-1341
Abstract:
A fengycin synthetase gene, fenB , has been cloned and sequenced. The protein (FenB) encoded by this gene has a predicted molecular mass of 143.6 kDa. This protein was overexpressed in Escherichia coli and was purified to near homogeneity by affinity chromatography. Experimental results indicated that the recombinant FenB has a substrate specificity toward isoleucine with an optimum temperature of 25°C, an optimum pH of 4.5, a K m value of 922 μM, and a turnover number of 236 s −1 . FenB also consists of a thioesterase domain, suggesting that this protein may be involved in the activation of the last amino acid of fengycin.
Type of Medium:
Online Resource
ISSN:
0021-9193
,
1098-5530
DOI:
10.1128/JB.180.5.1338-1341.1998
Language:
English
Publisher:
American Society for Microbiology
Publication Date:
1998
detail.hit.zdb_id:
1481988-0
SSG:
12
Bookmarklink