Article
Comparative kinetics of cofactor association and dissociation for the human and trypanosomal S-adenosylhomocysteine hydrolases. 2. The role of helix 18 stability.
Biochemistry - 29 Apr 2008
Li Qing-Shan, Cai Sumin, Fang Jianwen, Borchardt Ronald T, Kuczera Krzysztof, Middaugh C Russell, Schowen Richard L
Abstract excerpt
The S-adenosyl- l-homocysteine (AdoHcy) hydrolases (SAHH) from Homo sapiens (Hs-SAHH) and from the parasite Trypanosoma cruzi (Tc-SAHH) are very similar in structure and catalytic properties but differ in the kinetics and thermodynamics of association and dissociation of the cofactor NAD (+). The binding of NAD (+) and NADH in SAHH appears structurally to be mediated by helix 18, formed by seven residues near the...
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