Journal
JOURNAL OF BIOSCIENCE AND BIOENGINEERING
Volume 110, Issue 1, Pages 39-41Publisher
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
- MEXT Center for Practical Chemical Wisdom
- Waseda University [2009B-116, 2009A-893]
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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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