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Title: Single amino acid changes outside the active site significantly affect activity of glutathione S-transferases
Authors: Albert J. Ketterman
Peerada Prommeenate
Chanikarn Boonchauy
Umnaj Chanama
Somphop Leetachewa
Nongkran Promtet
La aied Prapanthadara
Mahidol University
The Institute of Science and Technology for Research and Development, Mahidol University
Chiang Mai University
Keywords: Agricultural and Biological Sciences;Biochemistry, Genetics and Molecular Biology
Issue Date: 1-Jan-2001
Citation: Insect Biochemistry and Molecular Biology. Vol.31, No.1 (2001), 65-74
Abstract: Glutathione S-transferases (GSTs: E.C. 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.
ISSN: 09651748
Appears in Collections:Scopus 2001-2005

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