TY - JOUR
T1 - Novel substrate specificity of glutathione synthesis enzymes from Streptococcus agalactiae and Clostridium acetobutylicum
AU - Kino, Kuniki
AU - Kuratsu, Shoko
AU - Noguchi, Atsushi
AU - Kokubo, Masahiro
AU - Nakazawa, Yuji
AU - Arai, Toshinobu
AU - Yagasaki, Makoto
AU - Kirimura, Kohtaro
PY - 2007/1/12
Y1 - 2007/1/12
N2 - 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.
AB - 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.
KW - Clostridium acetobutylicum
KW - Glutathione
KW - Glutathione synthetase
KW - Streptococcus agalactiae
KW - γ-Glutamylcysteine synthetase
KW - γ-Glutamylpeptide
UR - http://www.scopus.com/inward/record.url?scp=33751538620&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=33751538620&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2006.11.016
DO - 10.1016/j.bbrc.2006.11.016
M3 - Article
C2 - 17123467
AN - SCOPUS:33751538620
SN - 0006-291X
VL - 352
SP - 351
EP - 359
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -