Gh. Li et al., MOLECULAR-CLONING AND CHARACTERIZATION OF FENGYCIN SYNTHETASE GENE FENB FROM BACILLUS-SUBTILIS, Journal of bacteriology, 180(5), 1998, pp. 1338-1341
A fengycin synthetase gene, fenB, has been cloned and sequenced. The p
rotein (FenB) encoded by this gene has a predicted molecular mass of 1
43.6 kDa. This protein was overexpressed in Escherichia coli and was p
urified to near homogeneity by affinity chromatography. Experimental r
esults indicated that the recombinant FenB has a substrate specificity
toward isoleucine with an optimum temperature of 25 degrees C, an opt
imum pH of 4.5, a K-m value of 922 mu M, and a turnover number of 236
s(-1). FenB also consists of a thioesterase domain, suggesting that th
is protein mag be involved in tile activation of the last amino acid o
f fengycin.