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KMID : 0545120010110050798
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Journal of Microbiology and Biotechnology
2001 Volume.11 No. 5 p.798 ~ p.803
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A Putative Peptide Synthetase from Bacillus subtilis 713 Recognizing L-Lysine, L-Trytophan, and L-Glutamic Acid
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Kim, Kyoung Rok
Lee, In Hyung/Suh, Joo Won
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Abstract
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Peptide synthetases produced from various microorganisms are multifunctional enzyme complexes and their substrates are recognized and activated by adenylation domains. To identify the substrate specificity of the peptide synthetase isolated from Bacillus subtilis 713, known to produce an antifungal peptide, two adenylation domains containing the minimal functional portion were expressed and purified. ATP-ppi exchange experiments and kinetic studies revealed that the two adenylation enzymes had a substrate specificity to L-lysine and L-tryptophan, respectively. In addition, based on a signature sequence comparison, the substrate of the third domain was predicted to be L-glutamic acid. These results suggest that this peptide synthetase is novel because there has been no previous report on a peptide synthetase that uses L-lysine, L-tryptophan, and L-glutamic acid as substrates in that order.
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