Glutamyl adenylate analogues are inhibitors of glutamyl-tRNA synthetase

Michel Desjardins; Sylvie Garneau; Julie Desgagnés; Lucille Lacoste; Fu Yang; Jacques Lapointe; Robert Chênevert

doi:10.1006/bioo.1998.1082

Glutamyl adenylate analogues are inhibitors of glutamyl-tRNA synthetase

Michel Desjardins, Sylvie Garneau, Julie Desgagnés, Lucille Lacoste, Fu Yang, Jacques Lapointe, Robert Chênevert

Research output: Contribution to journal › Article › peer-review

19 Scopus citations

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	https://doi.org/10.1006/bioo.1998.1082
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.).

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Drug Discovery
Organic Chemistry

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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.",

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AU - Lacoste, Lucille

AU - Yang, Fu

AU - Lapointe, Jacques

AU - Chênevert, Robert

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Glutamyl adenylate analogues are inhibitors of glutamyl-tRNA synthetase

Abstract

Bibliographical note

ASJC Scopus subject areas

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