Glutathione mutagenesis in Salmonella typhimurium TA100: Dependence on a single enzyme, γ-glutamyltranspeptidase

Avishay Abraham Stark*, Errol Zeiger, Dennis A. Pagano

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

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

Original languageEnglish
Pages (from-to)45-52
Number of pages8
JournalMutation Research - Fundamental and Molecular Mechanisms of Mutagenesis
Volume177
Issue number1
DOIs
StatePublished - Mar 1987

Keywords

  • (Salmonella typhimurium)
  • Glutathione
  • Glycylglycine
  • Serine-borate complex
  • γ-Glutamyltranspeptidase

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