Stability of the domain interface contributes towards the catalytic function at the H-site of class alpha glutathione transferase A1-1

Article ID	Journal	Published Year	Pages	File Type
1179968	Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics	2010	6 Pages	PDF

Abstract

âº Trp21 is conserved at the domain interface of class alpha GSTs. âº W21A mutation compromises stability but not structure of domain interface. âº W21A mutant displays reduced catalytic function at the H-site. âº Domain interface stability is important for transition state stabilisation.

Keywords

GSH GST CDNB TNB Domain–domain interactions 1-chloro-2,4-dinitrobenzene 1,3,5-Trinitrobenzene 8-Anilino-1-naphthalene sulfonate Ethacrynic acid Transition state stabilization circular dichroism ANS Catalytic function Protein stability Glutathione Glutathione transferase

Related Topics

Physical Sciences and Engineering Chemistry Analytical Chemistry

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Stability of the domain interface contributes towards the catalytic function at the H-site of class alpha glutathione transferase A1-1

Authors

David Balchin, Sylvia Fanucchi, Ikechukwu Achilonu, Roslin J. Adamson, Jonathan Burke, Manuel Fernandes, Samantha Gildenhuys, Heini W. Dirr,