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Title: Novel substrate specificity of glutathione synthesis enzymes from Streptococcus agalactiae and Clostridium acetobutylicum

Abstract

Glutathione (GSH) is synthesized by {gamma}-glutamylcysteine synthetase ({gamma}-GCS) and glutathione synthetase (GS) in living organisms. Recently, bifunctional fusion protein, termed {gamma}-GCS-GS catalyzing both {gamma}-GCS and GS reactions from gram-positive firmicutes Streptococcus agalactiae, has been reported. We revealed that in the {gamma}-GCS activity, S. agalactiae {gamma}-GCS-GS had different substrate specificities from those of Escherichia coli {gamma}-GCS. Furthermore, S. agalactiae {gamma}-GCS-GS synthesized several kinds of {gamma}-glutamyltripeptide, {gamma}-Glu-X{sub aa}-Gly, from free three amino acids. In Clostridium acetobutylicum, the genes encoding {gamma}-GCS and putative GS were found to be immediately adjacent by BLAST search, and had amino acid sequence homology with S. agalactiae {gamma}-GCS-GS, respectively. We confirmed that the proteins expressed from each gene showed {gamma}-GCS and GS activity, respectively. C. acetobutylicum GS had broad substrate specificities and synthesized several kinds of {gamma}-glutamyltripeptide, {gamma}-Glu-Cys-X{sub aa}. Whereas the substrate specificities of {gamma}-GCS domain protein and GS domain protein of S. agalactiae {gamma}-GCS-GS were the same as those of S. agalactiae {gamma}-GCS-GS.

Authors:
 [1];  [2];  [2];  [2];  [2];  [2];  [3];  [2]
  1. Department of Applied Chemistry, School of Science and Engineering, Waseda University, Ohkubo 3-4-1, Shinjuku-ku, Tokyo 169-8555 (Japan). E-mail: kkino@waseda.jp
  2. Department of Applied Chemistry, School of Science and Engineering, Waseda University, Ohkubo 3-4-1, Shinjuku-ku, Tokyo 169-8555 (Japan)
  3. Kyowa Hakko Kogyo Co., Ltd., Technical Research Laboratories, 1-1 Kyowa-cho, Hofu-city, Yamaguchi 747-8522 (Japan)
Publication Date:
OSTI Identifier:
20857952
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 352; Journal Issue: 2; Other Information: DOI: 10.1016/j.bbrc.2006.11.016; PII: S0006-291X(06)02484-3; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; AMINO ACID SEQUENCE; AMINO ACIDS; BIOSYNTHESIS; CLOSTRIDIUM ACETOBUTYLICUM; ESCHERICHIA COLI; GENES; GLUTATHIONE; LIGASES; SPECIFICITY; STREPTOCOCCUS; SUBSTRATES

Citation Formats

Kino, Kuniki, Kuratsu, Shoko, Noguchi, Atsushi, Kokubo, Masahiro, Nakazawa, Yuji, Arai, Toshinobu, Yagasaki, Makoto, and Kirimura, Kohtaro. Novel substrate specificity of glutathione synthesis enzymes from Streptococcus agalactiae and Clostridium acetobutylicum. United States: N. p., 2007. Web. doi:10.1016/j.bbrc.2006.11.016.
Kino, Kuniki, Kuratsu, Shoko, Noguchi, Atsushi, Kokubo, Masahiro, Nakazawa, Yuji, Arai, Toshinobu, Yagasaki, Makoto, & Kirimura, Kohtaro. Novel substrate specificity of glutathione synthesis enzymes from Streptococcus agalactiae and Clostridium acetobutylicum. United States. doi:10.1016/j.bbrc.2006.11.016.
Kino, Kuniki, Kuratsu, Shoko, Noguchi, Atsushi, Kokubo, Masahiro, Nakazawa, Yuji, Arai, Toshinobu, Yagasaki, Makoto, and Kirimura, Kohtaro. Fri . "Novel substrate specificity of glutathione synthesis enzymes from Streptococcus agalactiae and Clostridium acetobutylicum". United States. doi:10.1016/j.bbrc.2006.11.016.
@article{osti_20857952,
title = {Novel substrate specificity of glutathione synthesis enzymes from Streptococcus agalactiae and Clostridium acetobutylicum},
author = {Kino, Kuniki and Kuratsu, Shoko and Noguchi, Atsushi and Kokubo, Masahiro and Nakazawa, Yuji and Arai, Toshinobu and Yagasaki, Makoto and Kirimura, Kohtaro},
abstractNote = {Glutathione (GSH) is synthesized by {gamma}-glutamylcysteine synthetase ({gamma}-GCS) and glutathione synthetase (GS) in living organisms. Recently, bifunctional fusion protein, termed {gamma}-GCS-GS catalyzing both {gamma}-GCS and GS reactions from gram-positive firmicutes Streptococcus agalactiae, has been reported. We revealed that in the {gamma}-GCS activity, S. agalactiae {gamma}-GCS-GS had different substrate specificities from those of Escherichia coli {gamma}-GCS. Furthermore, S. agalactiae {gamma}-GCS-GS synthesized several kinds of {gamma}-glutamyltripeptide, {gamma}-Glu-X{sub aa}-Gly, from free three amino acids. In Clostridium acetobutylicum, the genes encoding {gamma}-GCS and putative GS were found to be immediately adjacent by BLAST search, and had amino acid sequence homology with S. agalactiae {gamma}-GCS-GS, respectively. We confirmed that the proteins expressed from each gene showed {gamma}-GCS and GS activity, respectively. C. acetobutylicum GS had broad substrate specificities and synthesized several kinds of {gamma}-glutamyltripeptide, {gamma}-Glu-Cys-X{sub aa}. Whereas the substrate specificities of {gamma}-GCS domain protein and GS domain protein of S. agalactiae {gamma}-GCS-GS were the same as those of S. agalactiae {gamma}-GCS-GS.},
doi = {10.1016/j.bbrc.2006.11.016},
journal = {Biochemical and Biophysical Research Communications},
number = 2,
volume = 352,
place = {United States},
year = {Fri Jan 12 00:00:00 EST 2007},
month = {Fri Jan 12 00:00:00 EST 2007}
}