Molecular cloning and characterization of fengycin synthetase gene fenB from Bacillus subtilis |
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Authors: | GH Lin CL Chen JS Tschen SS Tsay YS Chang ST Liu |
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Affiliation: | Plastic and Reconstructive Surgery, Clark & Daughtrey Medical Group, P.A., Lakeland, Fla 33803, USA. |
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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 degrees C, an optimum pH of 4.5, a Km value of 922 microM, 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. |
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