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dc.contributor.authorAlbert J. Kettermanen_US
dc.contributor.authorPeerada Prommeenateen_US
dc.contributor.authorChanikarn Boonchauyen_US
dc.contributor.authorUmnaj Chanamaen_US
dc.contributor.authorSomphop Leetachewaen_US
dc.contributor.authorNongkran Promteten_US
dc.contributor.authorLa aied Prapanthadaraen_US
dc.contributor.otherMahidol Universityen_US
dc.contributor.otherThe Institute of Science and Technology for Research and Development, Mahidol Universityen_US
dc.contributor.otherChiang Mai Universityen_US
dc.date.accessioned2018-09-07T09:36:55Z-
dc.date.available2018-09-07T09:36:55Z-
dc.date.issued2001-01-01en_US
dc.identifier.citationInsect Biochemistry and Molecular Biology. Vol.31, No.1 (2001), 65-74en_US
dc.identifier.issn09651748en_US
dc.identifier.other2-s2.0-0035185961en_US
dc.identifier.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0035185961&origin=inwarden_US
dc.identifier.urihttp://repository.li.mahidol.ac.th/dspace/handle/123456789/26415-
dc.description.abstractGlutathione S-transferases (GSTs: E.C. 2.5.1.18) are a multigene family of multifunctional dimeric proteins that play a central role in detoxication. Four allelic forms of the mosquito Anopheles dirus GST, adGSTI-1, were cloned, expressed and characterized. The one or two amino acid changes in each allelic form was shown to confer different kinetic properties. Based on an available crystal structure, several of the residue changes were not in the putative substrate-binding pocket. Modeling showed that these insect Delta class GSTs also possess a hydrophobic surface pocket reported for Alpha, Mu and Pi class GSTs. The atom movement after replacement and minimization showed an average atom movement of about 0.1 Å for the 0 to 25 Å distance from the alpha carbon of the single replaced residue. This does not appear to be a significant movement in a static modeled protein structure. However, 200-500 atoms were involved with movements greater than 0.2 Å. Dynamics simulations were performed to study the effects this phenomenon would exert on the accessible conformations. The data show that residues affecting nearby responsive regions of tertiary structure can modulate enzyme specificities, possibly through regulating attainable configurations of the protein. © 2001 Elsevier Science Ltd.en_US
dc.rightsMahidol Universityen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0035185961&origin=inwarden_US
dc.subjectAgricultural and Biological Sciencesen_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.titleSingle amino acid changes outside the active site significantly affect activity of glutathione S-transferasesen_US
dc.typeArticleen_US
dc.rights.holderSCOPUSen_US
dc.identifier.doi10.1016/S0965-1748(00)00106-5en_US
Appears in Collections:Scopus 2001-2005

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