Human glutathione transferase A3-3 active as steroid double-bond isomerase.
Glutathione transferases (GSTs) constitute a superfamily of detoxifying enzymes with a major role in protecting cellular macromolecules from reactive electrophilic compounds. A growing body of evidence suggests, however, that at least certain glutathione transferases are involved in other essential cellular processes, such as cellular signaling and anabolic pathways. One of them is the human GST A3-3, which is selectively expressed in steroidogenic organs and which efficiently catalyzes the obligatory isomerization of the Delta(5)-ketosteroid precursors in the biosynthesis of progesterone and testosterone. In this chapter, we summarize the current knowledge on human GST A3-3 and describe methods for heterologous expression and functional characterization of the enzyme.
Raffalli-Mathieu
Françoise
F
Department of Biochemistry, Uppsala University Biomedical Center, Sweden.
Mannervik
Bengt
B
D017398:Alternative Splicing; D000595:Amino Acid Sequence; D000818:Animals; D003001:Cloning, Molecular; D005982:Glutathione Transferase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D007527:Isoenzymes / Q000235:genetics / Q000378:metabolism; D007535:Isomerases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D015394:Molecular Structure; D013256:Steroids / Q000737:chemistry / Q000378:metabolism*; D014018:Tissue Distribution
D007527:Isoenzymes; D013256:Steroids; D005982:Glutathione Transferase; C495975:glutathione S-transferase A3-3, human; D007535:Isomerases