PMID:9495777

Citation	Lin, GH, Chen, CL, Tschen, JS, Tsay, SS, Chang, YS and Liu, ST (1998) Molecular cloning and characterization of fengycin synthetase gene fenB from Bacillus subtilis. J. Bacteriol. 180:1338-41
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.
Links	PubMed PMC107026
Keywords	Amino Acid Sequence; Aminoacylation; Antifungal Agents/biosynthesis; Bacillus subtilis/enzymology; Bacillus subtilis/genetics; Chromatography, Affinity; Cloning, Molecular; Escherichia coli/genetics; Genes, Bacterial; Hydrogen-Ion Concentration; Isoleucine/metabolism; Kinetics; Lipopeptides; Lipoproteins/biosynthesis; Molecular Sequence Data; Molecular Weight; Peptide Synthases/chemistry; Peptide Synthases/genetics; Peptide Synthases/isolation & purification; Peptide Synthases/metabolism; Recombinant Proteins/chemistry; Recombinant Proteins/isolation & purification; Recombinant Proteins/metabolism; Substrate Specificity; Temperature
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
BACSU:Q45563		GO:0008152: metabolic process	ECO:0000314:		P		Table 2. Used various amino acids with fenB to determine exchange activity between the isotope labelled amino acids and ATP-PPi.	complete

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