Identification and characterization of GSTT3, a third murine Theta class glutathione transferase.
A novel Theta class glutathione transferase (GST) isoenzyme from mouse termed mGSTT3 has been identified by analysis of the expressed sequence tag database. The gene encoding mGSTT3 is clustered with the mGSTT1 and mGSTT2 genes on chromosome 10 and has an exon/intron structure that is similar to that of the other Theta class genes. mGSTT3 is expressed strongly in the liver and to a decreasing extent in the kidney and testis. Recombinant mGSTT3-3 expressed in Escherichia coli had a substrate-specificity profile that differed significantly from that of GSTT1-1 and GSTT2-2 isoenzymes. A molecular model of mGSTT3 suggested that, in comparison with GSTT2, a decrease in volume of the hydrophobic substrate-binding site and the loss of the sulphate-binding pocket prevents its use of the GSTT2 substrate 1-menaphthyl sulphate.
Coggan
Marjorie
M
Molecular Genetics Group, John Curtin School of Medical Research, Australian National University, P.O. Box 334, Canberra, Australian Capital Territory, 2601, Australia.
Flanagan
Jack U
JU
Parker
Michael W
MW
Vichai
Vanicha
V
Pearson
William R
WR
Board
Philip G
PG
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D015139:Blotting, Southern; D019992:Databases as Topic; D004926:Escherichia coli / Q000201:enzymology; D005091:Exons; D005982:Glutathione Transferase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D007438:Introns; D051379:Mice; D008957:Models, Genetic; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity; D014018:Tissue Distribution
D011994:Recombinant Proteins; C413545:glutathione S-transferase T1; D005982:Glutathione Transferase