Glutathione S-transferases, class Zeta , C-terminal (IPR034330)

Short name: GST_Zeta_C

Overlapping homologous superfamilies

Domain relationships


This entry represents the C-terminal domain of the glutathione S-transferase (GST) class Zeta subfamily members.

GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain [PMID: 15607001, PMID: 15069639].

Class Zeta GSTs, also known as maleylacetoacetate (MAA) isomerases, catalyze the isomerization of MAA to fumarylacetoacetate, the penultimate step in tyrosine/phenylalanine catabolism, using GSH as a cofactor [PMID: 12052898, PMID: 11352584]. They show little GSH-conjugating activity towards traditional GST substrates, but display modest GSH peroxidase activity [PMID: 9396740]. They are also implicated in the detoxification of the carcinogen dichloroacetic acid by catalyzing its dechlorination to glyoxylic acid [PMID: 9815194].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.