Journal article

Publication year: 2009

Pages: 115-122

Journal: Archives of Biochemistry and Biophysics

Volume number: 487

Issue number: 2

ISSN: 0003-9861

DOI Link: https://doi.org/10.1016/j.abb.2009.05.011

Publisher: Elsevier

Abstract: 
Glutathione S-transferases (GSTs) of Plasmodium parasites are potential targets for antimalarial drug and vaccine development. We investigated the equilibrium unfolding, functional activity regulation and stability characteristics of the unique GST of Plasmodium vivax (PvGST). Despite high sequence, Structural, functional, and evolutionary similarity, the unfolding behavior of PvGST was significantly different from Plasmodium falciparum GST (PfGST). The unfolding pathway of PvGST was non-cooperative with stabilization of an inactive dimeric intermediate. The absence of any compact, folded monomeric intermediate during the unfolding transition suggests that inter-subunit interactions play an important role in stabilizing the protein. Presence of salts effectively inhibited PvGST enzymatic activity by quenching the nucleophilicity of the thiolate anion of GSH. Based oil the present findings, together with Our previous Studies on PfGST, we propose that the regulation of GST enzymatic activity through a dimer-tetramer transition via GSH binding is an exclusive feature of Plasmodium. (C) 2009 Elsevier Inc. All rights reserved.

Harvard Citation style: Tripathi, T., Na, B., Sohn, W., Becker, K. and Bhakuni, V. (2009) Structural, functional and unfolding characteristics of glutathione S-transferase of Plasmodium vivax, Archives of Biochemistry and Biophysics, 487(2), pp. 115-122. https://doi.org/10.1016/j.abb.2009.05.011

APA Citation style: Tripathi, T., Na, B., Sohn, W., Becker, K., & Bhakuni, V. (2009). Structural, functional and unfolding characteristics of glutathione S-transferase of Plasmodium vivax. Archives of Biochemistry and Biophysics. 487(2), 115-122. https://doi.org/10.1016/j.abb.2009.05.011