A novel L-amino acid ligase from bacillus subtilis NBRC3134 catalyzed oligopeptide synthesis

Kuniki Kino*, Toshinobu Arai, Daisuke Tateiwa

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

20 Citations (Scopus)


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-oligo-mers 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.

Original languageEnglish
Pages (from-to)129-134
Number of pages6
JournalBioscience, Biotechnology and Biochemistry
Issue number1
Publication statusPublished - 2010


  • L-amino acid ligase
  • Oligopeptide synthesis
  • Rhizocticin

ASJC Scopus subject areas

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


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