Glutathione conjugation as a bioactivation reaction
article
In general, glutathione conjugation is regarded as a detoxication reaction. However, depending on the properties of the substrate, bioactivation is also possible. Four types of activation reaction have been recognized: direct-acting compounds, conjugates that are activated through cysteine conjugate beta-lyase, conjugates that are activated through redox cycling and lastly conjugates that release the original reactive parent compound. The glutathione S-transferases have three connections with the formation of biactivated conjugates: they catalyze their formation in a number of cases, they are the earliest available target for covalent binding by these conjugates and lastly, the parent alkylating agents are regularly involved in the induction of the enzymes. Individual susceptibility for each of these agents is determined by individual transferase subunit composition and methods are becoming available to assess this susceptibility. © 2000 Elsevier Science Ireland Ltd. Chemicals/CAS: Carbon-Sulfur Lyases, EC 4.4.-; Glutathione Transferase, EC 2.5.1.18; Glutathione, 70-18-8; S-alkylcysteine lyase, EC 4.4.1.6; Xenobiotics
Topics
BioactivationGlutathione conjugatesGlutathione S-transferasesCysteineGlutathioneGlutathione transferaseLyaseCatalysisChemical bindingChemical reactionChromosomal localizationConjugationCovalent bondDetoxificationEnzyme activationEnzyme activityEnzyme inductionEnzyme inhibitionEnzyme mechanismGene locationGenetic polymorphismHumanNonhumanProtein expressionReaction analysisReductionAnimalsBiotransformationCarbon-Sulfur LyasesEnzyme InductionGlutathioneGlutathione TransferaseHumansMetabolic Detoxication, DrugOxidation-ReductionXenobiotics
TNO Identifier
56919
ISSN
00092797
Source
Chemico-Biological Interactions, 129(1-2), pp. 61-76.
Pages
61-76
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