Evaluation of NAD (H) analogues as selective inhibitors for Trypanosoma cruzi S-adenosylhomocysteine hydrolase

…, RT Borchardt, K Kuczera, CR Middaugh…

Index: Li, Qing-Shan; Cai, Sumin; Fang, Jianwen; Borchardt, Ronald T.; Kuczera, Krzysztof; Middaugh, C. Russell; Schowen, Richard L. Nucleosides, Nucleotides and Nucleic Acids, 2009 , vol. 28, # 5-7 p. 473 - 484

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Citation Number: 4

Abstract

S-Adenosylhomocysteine (AdoHcy) hydrolases (SAHHs) from human sources (Hs-SAHHs) bind the cofactor NAD+ more tightly than several parasitic SAHHs by around 1000-fold. This property suggests the cofactor binding site of this essential enzyme as a potential anti- parasitic drug target, eg, against SAHH from Trypansoma cruzi (Tc-SAHH). The on-rate and off-rate constants and the equilibrium dissociation constants were determined for NAD+/ ...