Identification and characterization of a novel L-amino acid ligase from Photorhabdus luminescens subsp. laumondii TT01.
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.
Kino
Kuniki
K
Department of Applied Chemistry, Faculty of Science and Engineering, Waseda University, 3-4-1 Ohkubo, Shinjuku-ku, Tokyo 169-8555, Japan. kkino@waseda.jp
Noguchi
Atsushi
A
Arai
Toshinobu
T
Yagasaki
Makoto
M
D000596:Amino Acids / Q000378:metabolism*; D001216:Asparagine / Q000378:metabolism; D004151:Dipeptides / Q000378:metabolism; D008025:Ligases / Q000378:metabolism*; D020637:Photorhabdus / Q000201:enzymology*; D013379:Substrate Specificity
D000596:Amino Acids; D004151:Dipeptides; D001216:Asparagine; D008025:Ligases