| Autor: |
Wang, M., Zhang, J., Andrei, D., Kuczera, K., Borchardt, R. T., Wnuk, S. F. |
| Zdroj: |
Journal of Medicinal Chemistry; January 2005, Vol. 48 Issue: 10 p3649-3653, 5p |
| Abstrakt: |
Moffatt oxidation of 2,3-O-isopropylidene-l-adenosine and treatment of the resulting crude 5-aldehyde with hydroxylamine followed by deprotection gave l-adenosine 5-carboxaldehyde oximes, whose enantiomers are known to be potent inhibitors of S-adenosyl-l-homocysteine (AdoHcy) hydrolase. The l-adenosine and its 5-aldehyde oxime derivatives were found to be inactive as inhibitors of AdoHcy hydrolase. Docking calculations showed that binding of l-adenosine to AdoHcy hydrolase is weaker (higher energy) and less specific (larger number of clusters) compared to d-Ado. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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