Abstract
Glutamol adenylate 10 was a competitive inhibitor (K(i) = 3 μM) of glutamyl-tRNA synthetase from Escherichia coli. The N6-benzoyl adenine derivative 9 was also an inhibitor (K(i) ~ 60 μM). Replacement of adenine by other bases (purine, cytosine, dihydrocytosine, uridine) resulted in a more than 1000-fold loss in activity, indicating the important contribution of the adenine ring to the enzyme binding.
| Original language | English |
|---|---|
| Pages (from-to) | 1-13 |
| Number of pages | 13 |
| Journal | Bioorganic Chemistry |
| Volume | 26 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jun 1998 |
Bibliographical note
Funding Information:This work was supported by Grants OGP0009597 (to J.L.) and CPG0164048 (to R.C. and J.L.) from the Natural Sciences and Engineering Research Council of Canada and by Grant 98-ER-2481 from the ‘‘Fonds FCAR du Ministère de l’Éducation du Québec’’ (to R.C. and J.L.).
Funding
This work was supported by Grants OGP0009597 (to J.L.) and CPG0164048 (to R.C. and J.L.) from the Natural Sciences and Engineering Research Council of Canada and by Grant 98-ER-2481 from the ‘‘Fonds FCAR du Ministère de l’Éducation du Québec’’ (to R.C. and J.L.).
| Funders | Funder number |
|---|---|
| Ministère de l'Éducation, du Loisir et du Sport Québec | |
| Natural Sciences and Engineering Research Council of Canada | 98-ER-2481 |
| Fonds pour la Formation de Chercheurs et l'Aide à la Recherche |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Drug Discovery
- Organic Chemistry