New L-Amino acid ligases catalyzing oligopeptide synthesis from various microorganisms

Toshinobu Arai, Kuniki Kino

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

L-Amino acid ligase synthesizes various peptides from unprotected L-amino acids in an ATP-dependent manner. Known L-amino acid ligases catalyze only dipeptide synthesis, but recently we found that RizB of Bacillus subtilis NBRC 3134 catalyzes oligopeptide synthesis. In the present study, we searched for new members of the L-amino acid ligase group that catalyze oligopeptide synthesis. Several hypothetical proteins possessing the ATP-grasp motif were selected by in silico analysis. These recombinant proteins were assayed for L-amino acid ligase activity. We obtained five L-amino acid ligases showing oligopeptide synthesis activities. These proteins showed low similarity in amino acid sequence, but commonly used branched-chain amino acids, such as RizB, as substrates. Furthermore, the spr0969 protein of Streptococcus pneumoniae synthesized longer peptides than those synthesized by RizB, and the BAD 1200 protein of Bifidobacterium adolescentis showed higher activity toward aromatic amino acids than toward branched-chain ones. We also examined some of their characteristics.

Original languageEnglish
Pages (from-to)1572-1577
Number of pages6
JournalBioscience, Biotechnology and Biochemistry
Volume74
Issue number8
DOIs
Publication statusPublished - 2010 Sep 1

Keywords

  • In silico analysis
  • L-amino acid ligase
  • Oligopeptide
  • Peptide synthesis

ASJC Scopus subject areas

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

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