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Species-specific inhibition of Giardia lamblia triosephosphate isomerase by localized perturbation of the homodimer.

Abstract：

:Giardia lamblia depends on glycolysis to obtain ATP, highlighting the suitability of glycolytic enzymes as targets for drug design. We studied triosephosphate isomerase from G. lamblia (GlTIM) as a potential species-specific drug target. Cysteine-reactive agents were used as probes, in order to test those regions near to cysteine residues as targets to perturb enzyme structure and activity. Methyl methanethiosulfonate (MMTS) derivatized three of the five Cys per subunit of dimeric GlTIM and induced 50% of inactivation. The 2-carboxyethyl methanethiosulfonate (MTSCE) modified four Cys and induced 97% of inactivation. Inactivation by MMTS or MTSCE did not affect secondary structure, nor induce dimer dissociation; however, Cys modification decreased thermal stability of enzyme. Inactivation and dissociation of the dimer to stable monomers were reached when four Cys were derivatized by 5,5'-dithio-bis(2-nitrobenzoic acid) (DTNB). The effects of DTNB were completely abolished when GlTIM was first treated with MMTS. The effect of thiol reagents on human TIM was also assayed; it is 180-fold less sensitive than GlTIM. Collectively, the data illustrate GlTIM as a good target for drug design.

journal_name

Mol Biochem Parasitol

journal_title

Molecular and biochemical parasitology

authors

Enriquez-Flores S,Rodriguez-Romero A,Hernandez-Alcantara G,De la Mora-De la Mora I,Gutierrez-Castrellon P,Carvajal K,Lopez-Velazquez G,Reyes-Vivas H

doi

10.1016/j.molbiopara.2007.10.013

subject

Has Abstract

pub_date

2008-02-01 00:00:00

pages

179-86

issue

2

eissn

0166-6851

issn

1872-9428

pii

S0166-6851(07)00306-4

journal_volume

157

pub_type

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