A Novel L-Amino Acid Ligase from Bacillus subtilis NBRC3134 Catalyzed Oligopeptide Synthesis
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概要
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L-Amino acid ligase catalyzes dipeptide synthesis from unprotected L-amino acids in an ATP-dependent manner. We have purified a new L-amino acid ligase, RizA, which synthesizes dipeptides whose N-terminus is Arg, from Bacillus subtilis NBRC3134, a microorganism that produces a rhizocticin peptide antibiotic. It was suggested that RizA is probably involved in rhizocticin biosynthesis. In this study, we performed sequence analysis of unknown regions around rizA, and newly identified a gene that encodes a protein that possesses an ATP-grasp motif upstream of rizA. This gene was designated rizB, and its recombinant protein was prepared. Recombinant RizB synthesized homo-oligomers of branched-chain L-amino acids and L-methionine consisting of two to five amino acids in an ATP-dependent manner. RizB also synthesized various heteropeptides. Further examination showed that RizB might elongate a peptide chain at the N-terminus. This is the first report on an L-amino acid ligase catalyzing oligopeptide synthesis.
- 社団法人 日本農芸化学会の論文
- 2010-01-23
著者
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Kino Kuniki
Department Of Applied Chemistry Faculty Of Science And Engineering Waseda University
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Arai Toshinobu
Department Of Applied Chemistry Faculty Of Science And Engineering Waseda University
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TATEIWA Daisuke
Department of Applied Chemistry, Faculty of Science and Engineering, Waseda University
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Tateiwa Daisuke
Department Of Applied Chemistry Faculty Of Science And Engineering Waseda University
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