A Novel L-Amino Acid Ligase from Bacillus subtilis NBRC3134, a Microorganism Producing Peptide-Antibiotic Rhizocticin
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概要
- 論文の詳細を見る
L-Amino acid ligase catalyzes the formation of an α-peptide bond from unprotected L-amino acids in an ATP-dependent manner, and this enzyme is very useful in efficient peptide production. We performed enzyme purification to obtain a novel L-amino acid ligase from Bacillus subtilis NBRC3134, a microorganism producing peptide-antibiotic rhizocticin. Rhizocticins are dipeptide or tripeptide antibiotics and commonly possess L-arginyl-L-2-amino-5-phosphono-3-cis-pentenoic acid. The purification was carried out by detecting L-arginine hydroxamate synthesis activity, and a target enzyme was finally purified 1,280-fold with 0.8% yield. The corresponding gene was then cloned and designated rizA. rizA was 1,242 bp and coded for 413 amino acid residues. Recombinant RizA was prepared, and it was found that the recombinant RizA synthesized dipeptides whose N-terminus was L-arginine in an ATP-dependent manner. RizA had strict substrate specificity toward L-arginine as the N-terminal substrate; on the other hand, the substrate specificity at the C-terminus was relaxed.
- 社団法人 日本農芸化学会の論文
- 2009-04-23
著者
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Kino Kuniki
Department of Applied Chemistry, Faculty of Science and Engineering, Waseda University
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Kino Kuniki
Dep. Of Applied Chemistry Fac. Of Sci. And Engineering Waseda Univ.
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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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Yagasaki Makoto
Technical Research Laboratories Kyowa Hakko Bio Co. Ltd.
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Arai Toshinobu
Dep. Of Applied Chemistry Fac. Of Sci. And Engineering Waseda Univ.
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KOTANAKA Yoichi
Department of Applied Chemistry, Faculty of Science and Engineering, Waseda University
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Kotanaka Yoichi
Department Of Applied Chemistry Faculty Of Science And Engineering Waseda University
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