4.4 Article

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

Journal

JOURNAL OF BIOSCIENCE AND BIOENGINEERING
Volume 110, Issue 1, Pages 39-41

Publisher

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

Keywords

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

Funding

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

Ask authors/readers for more resources

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.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.4
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available