Journal of Microbiology and Biotechnology

  • 제11권5호
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  • Pages.798-803
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  • 2001
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  • 1017-7825(pISSN)
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  • 1738-8872(eISSN)
한국미생물·생명공학회 (The Korean Society for Microbiology and Biotechnology)
권호 표지

A Putative Peptide Synthetase from Bacillus subtilis 713 Recognizing $_{L}-Lysine,{\;}_{L}-Tryptophan,{\;}and{\;}_{L}-Glutamic$ Acid

  • Kim, Kyoung-Rok (Institute of Bioscience and Biotechnology, Department of Biological Science, Myong Ji University) ;
  • Lee, In-Hyung (Department of Foods and Nutrition, Kookmin University) ;
  • Suh, Joo-Won (Institute of Bioscience and Biotechnology, Department of Biological Science, Myong Ji University)
  • 발행 : 2001.10.01
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초록

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.

키워드

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