Phylogenies of glutathione transferase families.
The best known glutathione transferase family, with its class-alpha, -mu, -pi, -omega, -sigma, -theta, and -zeta subdivisions, is only one of four, or perhaps five, ancient protein families that conjugate glutathione or use a glutathione intermediate: (1) the cytoplasmic family, (2) the mitochondrial (kappa) family, (3) the microsomal (MAPEG) family, which may actually be two separate families, and (4) the fosphomycin/glyoxalase family. Although the cytoplasmic family is perhaps the most diverse, all four of these families have homologs in both prokaryotes and eukaryotes; it is striking that at least three, and perhaps as many as five, different protein folds capable of binding and positioning glutathione for a nucleophilic attack emerged more than 2 billion years ago. This chapter presents phylogenies for the four (or five) glutathione transferase families, focusing on the statistical evidence for homology (and non-homology).
Pearson
William R
WR
Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, Virginia, USA.
D000818:Animals; D003593:Cytoplasm / Q000201:enzymology; D019143:Evolution, Molecular; D005982:Glutathione Transferase / Q000737:chemistry / Q000145:classification* / Q000235:genetics; D006801:Humans; D007527:Isoenzymes / Q000737:chemistry / Q000145:classification* / Q000235:genetics; D008861:Microsomes / Q000201:enzymology; D005810:Multigene Family; D010802:Phylogeny; D013879:Thioredoxins / Q000145:classification / Q000235:genetics
D007527:Isoenzymes; D013879:Thioredoxins; D005982:Glutathione Transferase