4.4 Article

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

期刊

JOURNAL OF BIOSCIENCE AND BIOENGINEERING
卷 110, 期 1, 页码 39-41

出版社

SOC BIOSCIENCE BIOENGINEERING JAPAN
DOI: 10.1016/j.jbiosc.2009.12.004

关键词

L-Amino acid ligase; Dipeptide; Photorhabdus luminescens; In silico screening; Enzymatic peptide synthesis

资金

  1. MEXT Center for Practical Chemical Wisdom
  2. Waseda University [2009B-116, 2009A-893]

向作者/读者索取更多资源

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. (C) 2009, The Society for Biotechnology, japan. All rights reserved.

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