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J Bacteriol, March 1998, p. 1338-1341, Vol. 180, No. 5
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Molecular Cloning and Characterization of Fengycin Synthetase Gene fenB from Bacillus subtilis

Guang-Huey Lin,1,2 Chyi-Liang Chen,2 Johannes Scheng-Ming Tschen,3 San-San Tsay,1 Yu-Sun Chang,2 and Shih-Tung Liu2,*

Graduate Institute of Botany, National Taiwan University, Taipei, 106,1 Graduate Institute of Botany, National Chung-Hsing University, Taichung, 402,3 and Molecular Genetics Laboratory, Department of Microbiology and Immunology, Chang-Gung University, Kwei-Shan, Taoyuan, 333,2 Taiwan

Received 3 November 1997/Accepted 30 December 1997

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 Km 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.

* Corresponding author. Molecular Genetics Laboratory, Department of Microbiology and Immunology, Chang-Gung University, Kwei-Shan, Taoyuan, 333, Taiwan. Phone: 886-3-328-0292. Fax: 886-3-328-0292. E-mail: cgliu{at}cguaplo.cgu.edu.tw.




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