Inactivation of polymorphic variants of human glutathione transferase zeta (hGSTZ1-1) by maleylacetone and fumarylacetone

Hoffman B.M. Lantum*, Philip G. Board, M. W. Anders

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    Abstract

    Glutathione transferase zeta (GSTZ1-1), 1 which is identical to maleylacetoacetate isomerase (EC 5.2.1.2) 2 is the penultimate enzyme in the tyrosine degradation pathway. GSTZ1-1 catalyzes the glutathione (GSH)-dependent cis-trans isomerization of maleylacetoacetate (MAA) to fumarylacetoacetate (FAA). Maleylacetone (MA), a decarboxylation product of MAA, is a substrate for the Vibrio 01 isomerase and is converted to fumarylacetone (FA). 3 No other endogenous role for GSTZ1-1 is known, but GSTZ1-1 also catalyzes the GSH-dependent biotransformation of a range of a-haloacids, such as dichloroacetic acid (DCA) and chlorofluoroacetic acid (CFA) 4
    Original languageEnglish
    Pages (from-to)339-342
    Number of pages4
    JournalAdvances in Experimental Medicine and Biology
    Volume500
    DOIs
    Publication statusPublished - 2001

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