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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Glutathione mutagenesis in Salmonella typhimurium TA100: dependence on a single enzyme, gamma-glutamyltranspeptidase.

Glutathione was mutagenic in Salmonella typhimurium strain TA100 in the presence of purified mammalian gamma-glutamyltranspeptidase. Glutathione disulfide, gamma-glutamyl glutamic acid, and S-methyl-glutathione were not mutagenic under the same conditions. Glutathione-mediated, gamma-glutamyltranspeptidase-dependent mutagenesis of TA100 cells was inhibited by serine-borate complex, a known gamma-glutamyltranspeptidase inhibitor, and potentiated by glycylglycine, a known gamma-glutamyltranspeptidase enhancer. It is concluded that this enzyme is necessary and sufficient to activate glutathione to a mutagen.[1]

References

  1. Glutathione mutagenesis in Salmonella typhimurium TA100: dependence on a single enzyme, gamma-glutamyltranspeptidase. Stark, A.A., Zeiger, E., Pagano, D.A. Mutat. Res. (1987) [Pubmed]
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