Glutathione-binding site of a bombyx mori theta-class glutathione transferase.
The glutathione transferase (GST) superfamily plays key roles in the detoxification of various xenobiotics. Here, we report the isolation and characterization of a silkworm protein belonging to a previously reported theta-class GST family. The enzyme (bmGSTT) catalyzes the reaction of glutathione with 1-chloro-2,4-dinitrobenzene, 1,2-epoxy-3-(4-nitrophenoxy)-propane, and 4-nitrophenethyl bromide. Mutagenesis of highly conserved residues in the catalytic site revealed that Glu66 and Ser67 are important for enzymatic function. These results provide insights into the catalysis of glutathione conjugation in silkworm by bmGSTT and into the metabolism of exogenous chemical agents.
Faculty of Agriculture, Kyushu University Graduate School, Fukuoka, Japan.
M D Tofazzal
MD
Hossain
Faculty of Agriculture, Kyushu University Graduate School, Fukuoka, Japan.
Naotaka
N
Yamada
Faculty of Agriculture, Kyushu University Graduate School, Fukuoka, Japan.
Kohji
K
Yamamoto
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D055162:Biocatalysis; D012831:Bombyx / Q000201:enzymology*; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics; D005978:Glutathione / Q000378:metabolism*; D005982:Glutathione Transferase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D015262:Xenobiotics / Q000378:metabolism
D018076:DNA, Complementary; D015262:Xenobiotics; D005982:Glutathione Transferase; D005978:Glutathione