Identification and characterization of a novel l-amino acid ligase from Photorhabdus luminescens subsp. laumondii TT01

Kuniki Kino, Atsushi Noguchi, Toshinobu Arai, Makoto Yagasaki

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11 Citations (Scopus)


l-Amino acid ligase catalyzes dipeptide synthesis from unprotected l-amino acids in an ATP-dependent manner. We recently identified a new member of l-amino acid ligase, the plu1440 protein, from Photorhabdus luminescens subsp. laumondii TT01 by in silico analysis. This protein was found to synthesize dipeptides containing l-asparagine at the N-terminus, which is a novel substrate specificity.

Original languageEnglish
Pages (from-to)39-41
Number of pages3
JournalJournal of Bioscience and Bioengineering
Issue number1
Publication statusPublished - 2010 Jul 1



  • Dipeptide
  • Enzymatic peptide synthesis
  • In silico screening
  • Photorhabdus luminescens
  • l-Amino acid ligase

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

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