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

@article{Li2009EvaluationON,
  title={Evaluation of NAD(H) analogues as selective inhibitors for Trypanosoma cruzi S-adenosylhomocysteine hydrolase.},
  author={Qing-Shan Li and Sumin Cai and Jianwen Fang and Ronald T. Borchardt and Krzysztof Kuczera and C. Russell Middaugh and R. L. Schowen},
  journal={Nucleosides, nucleotides & nucleic acids},
  year={2009},
  volume={28 5},
  pages={473-84}
}
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, e.g., against SAHH from Trypansoma cruzi (Tc-SAHH). The on-rate and off-rate constants and the equilibrium dissociation constants were determined for NAD(+)/NADH analogues and suggested that NADH analogues were… CONTINUE READING
3 Citations
23 References
Similar Papers

References

Publications referenced by this paper.
Showing 1-10 of 23 references

Comparative kinetics of cofactor association and dissociation for the human and trypanosomal D ow nl oa de d by [ U ni ve rs ity o f M ic hi ga n] a t 2 2: 45 1 6 A pr il

  • Q.-S. Li, S. Cai, +4 authors R. L. Schowen
  • 2007
Highly Influential
9 Excerpts

Compar - ative kinetics of cofactor association and dissociation for the human and trypanosomal S - adenosylhomocysteine hydrolases . 2 . The role of helix 18 stability

  • C. S. Yuan, J. Yeh, S. Liu, R. T. Borchardt
  • Biochemistry
  • 2008

Basic features of the association and dissociation processes

  • Q.-S. Li, S. Cai, +4 authors R. Schowen
  • Biochemistry
  • 2007

Similar Papers

Loading similar papers…