A novel L-amino acid ligase from Bacillus subtilis NBRC3134, a microorganism producing peptide-antibiotic rhizocticin

Kuniki Kino*, Yoichi Kotanaka, Toshinobu Arai, Makoto Yagasaki

*この研究の対応する著者

研究成果: Article査読

49 被引用数 (Scopus)

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 dipep-tide 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.

本文言語English
ページ(範囲)901-907
ページ数7
ジャーナルBioscience, Biotechnology and Biochemistry
73
4
DOI
出版ステータスPublished - 2009

ASJC Scopus subject areas

  • バイオテクノロジー
  • 分析化学
  • 生化学
  • 応用微生物学とバイオテクノロジー
  • 分子生物学
  • 有機化学

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