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 in | Biochemical and biophysical research communications Vol. 352; no. 2; pp. 351 - 359 |
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| Main Authors | , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
12.01.2007
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| Subjects | |
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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. |
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| 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 |
| Author_xml | – sequence: 1 givenname: Kuniki surname: Kino fullname: Kino, Kuniki email: kkino@waseda.jp organization: Department of Applied Chemistry, School of Science and Engineering, Waseda University, Ohkubo 3-4-1, Shinjuku-ku, Tokyo 169-8555, Japan – sequence: 2 givenname: Shoko surname: Kuratsu fullname: Kuratsu, Shoko organization: Department of Applied Chemistry, School of Science and Engineering, Waseda University, Ohkubo 3-4-1, Shinjuku-ku, Tokyo 169-8555, Japan – sequence: 3 givenname: Atsushi surname: Noguchi fullname: Noguchi, Atsushi organization: Department of Applied Chemistry, School of Science and Engineering, Waseda University, Ohkubo 3-4-1, Shinjuku-ku, Tokyo 169-8555, Japan – sequence: 4 givenname: Masahiro surname: Kokubo fullname: Kokubo, Masahiro organization: Department of Applied Chemistry, School of Science and Engineering, Waseda University, Ohkubo 3-4-1, Shinjuku-ku, Tokyo 169-8555, Japan – sequence: 5 givenname: Yuji surname: Nakazawa fullname: Nakazawa, Yuji organization: Department of Applied Chemistry, School of Science and Engineering, Waseda University, Ohkubo 3-4-1, Shinjuku-ku, Tokyo 169-8555, Japan – sequence: 6 givenname: Toshinobu surname: Arai fullname: Arai, Toshinobu organization: Department of Applied Chemistry, School of Science and Engineering, Waseda University, Ohkubo 3-4-1, Shinjuku-ku, Tokyo 169-8555, Japan – sequence: 7 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 – sequence: 8 givenname: Kohtaro surname: Kirimura fullname: Kirimura, Kohtaro organization: Department of Applied Chemistry, School of Science and Engineering, Waseda University, Ohkubo 3-4-1, Shinjuku-ku, Tokyo 169-8555, Japan |
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| 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 |
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