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

Glutathione (GSH) is synthesized by γ-glutamylcysteine synthetase (γ-GCS) and glutathione synthetase (GS) in living organisms. Recently, bifunctional fusion protein, termed γ-GCS–GS catalyzing both γ-GCS and GS reactions from gram-positive firmicutes Streptococcus agalactiae, has been reported. We r...

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Published inBiochemical and biophysical research communications Vol. 352; no. 2; pp. 351 - 359
Main Authors Kino, Kuniki, Kuratsu, Shoko, Noguchi, Atsushi, Kokubo, Masahiro, Nakazawa, Yuji, Arai, Toshinobu, Yagasaki, Makoto, Kirimura, Kohtaro
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 12.01.2007
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Abstract Glutathione (GSH) is synthesized by γ-glutamylcysteine synthetase (γ-GCS) and glutathione synthetase (GS) in living organisms. Recently, bifunctional fusion protein, termed γ-GCS–GS catalyzing both γ-GCS and GS reactions from gram-positive firmicutes Streptococcus agalactiae, has been reported. We revealed that in the γ-GCS activity, S. agalactiae γ-GCS–GS had different substrate specificities from those of Escherichia coli γ-GCS. Furthermore, S. agalactiae γ-GCS–GS synthesized several kinds of γ-glutamyltripeptide, γ-Glu-Xaa-Gly, from free three amino acids. In Clostridium acetobutylicum, the genes encoding γ-GCS and putative GS were found to be immediately adjacent by BLAST search, and had amino acid sequence homology with S. agalactiae γ-GCS–GS, respectively. We confirmed that the proteins expressed from each gene showed γ-GCS and GS activity, respectively. C. acetobutylicum GS had broad substrate specificities and synthesized several kinds of γ-glutamyltripeptide, γ-Glu-Cys-Xaa. Whereas the substrate specificities of γ-GCS domain protein and GS domain protein of S. agalactiae γ-GCS–GS were the same as those of S. agalactiae γ-GCS–GS.
AbstractList 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(a) sub(a)-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(a) sub(a). 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.
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.
Glutathione (GSH) is synthesized by γ-glutamylcysteine synthetase (γ-GCS) and glutathione synthetase (GS) in living organisms. Recently, bifunctional fusion protein, termed γ-GCS–GS catalyzing both γ-GCS and GS reactions from gram-positive firmicutes Streptococcus agalactiae, has been reported. We revealed that in the γ-GCS activity, S. agalactiae γ-GCS–GS had different substrate specificities from those of Escherichia coli γ-GCS. Furthermore, S. agalactiae γ-GCS–GS synthesized several kinds of γ-glutamyltripeptide, γ-Glu-Xaa-Gly, from free three amino acids. In Clostridium acetobutylicum, the genes encoding γ-GCS and putative GS were found to be immediately adjacent by BLAST search, and had amino acid sequence homology with S. agalactiae γ-GCS–GS, respectively. We confirmed that the proteins expressed from each gene showed γ-GCS and GS activity, respectively. C. acetobutylicum GS had broad substrate specificities and synthesized several kinds of γ-glutamyltripeptide, γ-Glu-Cys-Xaa. Whereas the substrate specificities of γ-GCS domain protein and GS domain protein of S. agalactiae γ-GCS–GS were the same as those of S. agalactiae γ-GCS–GS.
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(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(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.
Author Kuratsu, Shoko
Nakazawa, Yuji
Kokubo, Masahiro
Kino, Kuniki
Yagasaki, Makoto
Kirimura, Kohtaro
Noguchi, Atsushi
Arai, Toshinobu
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  givenname: Makoto
  surname: Yagasaki
  fullname: Yagasaki, Makoto
  organization: Kyowa Hakko Kogyo Co., Ltd., Technical Research Laboratories, 1-1 Kyowa-cho, Hofu-city, Yamaguchi 747-8522, Japan
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  givenname: Kohtaro
  surname: Kirimura
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Issue 2
Keywords Clostridium acetobutylicum
γ-Glutamylcysteine synthetase
γ-Glutamylpeptide
Streptococcus agalactiae
Glutathione
Glutathione synthetase
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Snippet Glutathione (GSH) is synthesized by γ-glutamylcysteine synthetase (γ-GCS) and glutathione synthetase (GS) in living organisms. Recently, bifunctional fusion...
Glutathione (GSH) is synthesized by gamma-glutamylcysteine synthetase (gamma-GCS) and glutathione synthetase (GS) in living organisms. Recently, bifunctional...
Glutathione (GSH) is synthesized by gamma -glutamylcysteine synthetase ( gamma -GCS) and glutathione synthetase (GS) in living organisms. Recently,...
Glutathione (GSH) is synthesized by {gamma}-glutamylcysteine synthetase ({gamma}-GCS) and glutathione synthetase (GS) in living organisms. Recently,...
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SubjectTerms 60 APPLIED LIFE SCIENCES
AMINO ACID SEQUENCE
AMINO ACIDS
BIOSYNTHESIS
CLOSTRIDIUM ACETOBUTYLICUM
Clostridium acetobutylicum - classification
Clostridium acetobutylicum - enzymology
Enzyme Activation
ESCHERICHIA COLI
Firmicutes
GENES
GLUTATHIONE
Glutathione - chemistry
Glutathione Synthase - chemistry
Glutathione synthetase
LIGASES
Species Specificity
SPECIFICITY
STREPTOCOCCUS
Streptococcus agalactiae
Streptococcus agalactiae - classification
Streptococcus agalactiae - enzymology
Substrate Specificity
SUBSTRATES
γ-Glutamylcysteine synthetase
γ-Glutamylpeptide
Title Novel substrate specificity of glutathione synthesis enzymes from Streptococcus agalactiae and Clostridium acetobutylicum
URI https://dx.doi.org/10.1016/j.bbrc.2006.11.016
https://www.ncbi.nlm.nih.gov/pubmed/17123467
https://search.proquest.com/docview/19856151
https://search.proquest.com/docview/68369653
https://www.osti.gov/biblio/20857952
Volume 352
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