Simple jQuery Dropdowns
Please use this identifier to cite or link to this item:
Full metadata record
DC FieldValueLanguage
dc.contributor.authorRungrutai Udomsinpraserten_US
dc.contributor.authorSaengtong Pongjaroenkiten_US
dc.contributor.authorJantana Wongsantichonen_US
dc.contributor.authorAaron J. Oakleyen_US
dc.contributor.authorLa Aied Prapanthadaraen_US
dc.contributor.authorMatthew C J Wilceen_US
dc.contributor.authorAlbert J. Kettermanen_US
dc.contributor.otherMahidol Universityen_US
dc.contributor.otherMaejo Universityen_US
dc.contributor.otherUniversity of Western Australiaen_US
dc.contributor.otherChiang Mai Universityen_US
dc.identifier.citationBiochemical Journal. Vol.388, No.3 (2005), 763-771en_US
dc.description.abstractThe 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. © 2005 Biochemical Society.en_US
dc.rightsMahidol Universityen_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.titleIdentification, characterization and structure of a new Delta class glutathione transferase isoenzymeen_US
Appears in Collections:Scopus 2001-2005

Files in This Item:
There are no files associated with this item.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.