TY - JOUR
T1 - Identification and characterization of a novel l-amino acid ligase from Photorhabdus luminescens subsp. laumondii TT01
AU - Kino, Kuniki
AU - Noguchi, Atsushi
AU - Arai, Toshinobu
AU - Yagasaki, Makoto
N1 - Funding Information:
This work was supported in part by the Global COE program of the MEXT Center for Practical Chemical Wisdom and in part by a Waseda University Grant for Special Research , Project 2009B-116 and 2009A-893 .
PY - 2010/7
Y1 - 2010/7
N2 - 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.
AB - 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.
KW - Dipeptide
KW - Enzymatic peptide synthesis
KW - In silico screening
KW - Photorhabdus luminescens
KW - l-Amino acid ligase
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U2 - 10.1016/j.jbiosc.2009.12.004
DO - 10.1016/j.jbiosc.2009.12.004
M3 - Article
C2 - 20541113
AN - SCOPUS:77953104355
SN - 1389-1723
VL - 110
SP - 39
EP - 41
JO - Journal of Bioscience and Bioengineering
JF - Journal of Bioscience and Bioengineering
IS - 1
ER -