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Molecular cloning and characterization of fengycin synthetase gene fenB from Bacillus subtilis.


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.

SUBMITTER: Lin GH 

PROVIDER: S-EPMC107026 | biostudies-literature | 1998 Mar

REPOSITORIES: biostudies-literature

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Molecular cloning and characterization of fengycin synthetase gene fenB from Bacillus subtilis.

Lin G H GH   Chen C L CL   Tschen J S JS   Tsay S S SS   Chang Y S YS   Liu S T ST  

Journal of bacteriology 19980301 5


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). Fe  ...[more]

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