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• W2008827720 abstract "Trypanosomal S-adenoyl-L-homocysteine hydrolase (Tc-SAHH), considered as a target for treatment of Chagas disease, has the same catalytic mechanism as human SAHH (Hs-SAHH) and both enzymes have very similar x-ray structures. Efforts toward the design of selective inhibitors against Tc-SAHH targeting the substrate binding site have not to date shown any significant promise. Systematic kinetic and thermodynamic studies on association and dissociation of cofactor NAD/H for Tc-SAHH and Hs-SAHH provide a rationale for the design of anti-parasitic drugs directed toward cofactor-binding sites. Analogues of NAD and their reduced forms show significant selective inactivation of Tc-SAHH, confirming that this design approach is rational." @default.
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• W2008827720 date "2009-07-29" @default.
• W2008827720 modified "2023-09-26" @default.
• W2008827720 title "The Rationale for Targeting the NAD/NADH Cofactor Binding Site of Parasitic S-Adenosyl-L-Homocysteine Hydrolase for the Design of Anti-Parasitic Drugs" @default.
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• W2008827720 doi "https://doi.org/10.1080/15257770903051031" @default.
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