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

2006; Elsevier BV; Volume: 352; Issue: 2 Linguagem: Inglês

10.1016/j.bbrc.2006.11.016

1090-2104

Kuniki Kino, Shoko Kuratsu, Atsushi Noguchi, Masahiro Kokubo, Yuji Nakazawa, Toshinobu Arai, Makoto Yagasaki, Kohtaro Kirimura,

Redox biology and oxidative stress

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.