A Novel<scp>L</scp>-Amino Acid Ligase from<i>Bacillus subtilis</i>NBRC3134, a Microorganism Producing Peptide-Antibiotic Rhizocticin

DOI Web Site Web Site 被引用文献19件 参考文献29件
  • KINO Kuniki
    Department of Applied Chemistry, Faculty of Science and Engineering, Waseda University
  • KOTANAKA Yoichi
    Department of Applied Chemistry, Faculty of Science and Engineering, Waseda University
  • ARAI Toshinobu
    Department of Applied Chemistry, Faculty of Science and Engineering, Waseda University
  • YAGASAKI Makoto
    Technical Research Laboratories, Kyowa Hakko Bio Co., Ltd.

書誌事項

タイトル別名
  • A Novel L-Amino Acid Ligase from Bacillus subtilis NBRC3134, a Microorganism Producing Peptide-Antibiotic Rhizocticin

この論文をさがす

抄録

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.

収録刊行物

被引用文献 (19)*注記

もっと見る

参考文献 (29)*注記

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ