Designing of Species-specific inhibition: The cysteine residues of triosephosphate isomerase
Ashok Kumar Yadav, Kishore Kumar, Mukesh Verma, Mukesh Kumar, Manoj Kumar
Journal Title:Basic Research Journal of Medicine and Clinical Science
Enzymes from different species that have identical catalytic activities are usually very similar in their amino-acid sequences and three-dimensional structures. This is particularly true at the catalytic site, where the amino acids that form the active site and participate in catalysis are highly conserved. The similarities between homologous enzymes have hampered the design of species-specific inhibitors, in particular those directed toward the active centre. To circumvent this problem, attention has been given to regions that are close to the catalytic site but show individual structural features. This strategy has been used to design selective inhibitors against enzymes aimed at regions that are critical for enzyme stability.
Keywords: Triosephosphate isomerise, dihydroxyacetone phosphate (DHAP), cysteine, methylmethane thiosulphonate (MMTS), parasites.