title: Identification, characterization and structure of a new Delta class glutathione transferase isoenzyme.
abstract: The insect GST (glutathione transferase) supergene family encodes a varied group of proteins belonging to at least six individual classes. Interest in insect GSTs has focused on their role in conferring insecticide resistance. Previously from the mosquito malaria vector Anopheles dirus, two genes encoding five Delta class GSTs have been characterized for structural as well as enzyme activities. We have obtained a new Delta class GST gene and isoenzyme from A. dirus, which we name adGSTD5-5. The adGSTD5-5 isoenzyme was identified and was only detectably expressed in A. dirus adult females. A putative promoter analysis suggests that this GST has an involvement in oogenesis. The enzyme displayed little activity for classical GST substrates, although it possessed the greatest activity for DDT [1,1,1-trichloro-2,2-bis-(p-chlorophenyl)ethane] observed for Delta GSTs. However, GST activity was inhibited or enhanced in the presence of various fatty acids, suggesting that the enzyme may be modulated by fatty acids. We obtained a crystal structure for adGSTD5-5 and compared it with other Delta GSTs, which showed that adGSTD5-5 possesses an elongated and more polar active-site topology.
authors.affiliation: Institute of Molecular Biology and Genetics, Mahidol University, Salaya Campus, 25/25 Putthamonthol Road 4, Salaya, Nakon Pathom 73170, Thailand.
authors.forename: Rungrutai
authors.initials: R
authors.lastname: Udomsinprasert
authors.forename: Saengtong
authors.initials: S
authors.lastname: Pongjaroenkit
authors.forename: Jantana
authors.initials: J
authors.lastname: Wongsantichon
authors.forename: Aaron J
authors.initials: AJ
authors.lastname: Oakley
authors.forename: La-aied
authors.initials: LA
authors.lastname: Prapanthadara
authors.forename: Matthew C J
authors.initials: MC
authors.lastname: Wilce
authors.forename: Albert J
authors.initials: AJ
authors.lastname: Ketterman
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000852:Anopheles / Q000201:enzymology* / Q000235:genetics*; D001483:Base Sequence; D001665:Binding Sites; D018360:Crystallography, X-Ray; D018076:DNA, Complementary / Q000235:genetics / Q000302:isolation & purification; D023281:Genomics; D005982:Glutathione Transferase / Q000737:chemistry* / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D007527:Isoenzymes / Q000737:chemistry / Q000145:classification / Q000235:genetics / Q000378:metabolism; D007700:Kinetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011401:Promoter Regions, Genetic; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D055672:Static Electricity
chemical_list: D018076:DNA, Complementary; D007527:Isoenzymes; D011994:Recombinant Proteins; D005982:Glutathione Transferase
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