Triosephosphate

Plasmodium falciparumtriosephosphate isomerase (PfTIM) contains two tryptophan residues, W11 and W168. One is positioned in the interior of the protein, and the other is located on the active-site loop 6. Two single-tryptophan mutants, W11F and W168F, were constructed to evaluate the contributions of each chromophore to the fluorescence of the wild-type (wt) protein and to probe the utility of the residues as spectroscopic reporters.

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The synthesis of ATP in the human parasiteEntamoeba histolyticais car-ried out solely by the glycolytic pathway. Little kinetic and structural infor-mation is available for most of the pathway enzymes.

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The active site of triosephosphate isomerase (TIM, EC: 5.3.1.1), a dimeric enzyme, lies very close to the subunit interface. Attempts to engineer monomeric enzymes have yielded well-folded proteins with dra-matically reduced activity.

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Cys126 is a completely conserved residue in triosephosphate isomerase that is proximal to the active site but has been ascribed no specific role in catal-ysis. A previous study of the C126S and C126A mutants of yeast TIM reported substantial catalytic activity for the mutant enzymes, leading to the suggestion that this residue is implicated in folding and stability [Gonz-alez-Mondragon Eet al.

12p cosis54 05-01-2013 29 4   Download