Literature DB >> 9495777

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

G H Lin1, C L Chen, J S Tschen, S S Tsay, Y S Chang, S T Liu.   

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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Year:  1998        PMID： 9495777      PMCID： PMC107026          DOI： 10.1128/JB.180.5.1338-1341.1998

Source DB:  PubMed          Journal:  J Bacteriol        ISSN： 0021-9193            Impact factor:   3.490


  24 in total

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  6 in total

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