Alternative splicing of glutathione S-transferases.
This chapter discusses the alternative splicing of glutathione S-transferase proteins, including current investigations of enzymatic, nonenzymatic functions, as well as structural differences between the alternatively spliced products. The data demonstrate that the different GST splice forms possess different properties, both in their catalytic function and in the effects of their protein-protein interactions.
Wongsantichon
Jantana
J
Institute of Molecular Biology and Genetics, Mahidol University, Slaya, Nakhon Pathom, Thailand.
Ketterman
Albert J
AJ
D017398:Alternative Splicing; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D005091:Exons; D005982:Glutathione Transferase / Q000737:chemistry / Q000145:classification / Q000235:genetics / Q000378:metabolism; D006801:Humans; D007527:Isoenzymes / Q000737:chemistry / Q000145:classification / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D005810:Multigene Family; D011487:Protein Conformation; D021122:Protein Subunits / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment; D013379:Substrate Specificity
D007527:Isoenzymes; D021122:Protein Subunits; D005982:Glutathione Transferase