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.
|Number of pages||13|
|State||Published - Jun 1998|
Bibliographical noteFunding 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.).
ASJC Scopus subject areas
- Molecular Biology
- Drug Discovery
- Organic Chemistry