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Synthesis of an inhibitor of glutamyl-tRNA synthetase by Catherine Dorion; Robert Chênevert; Lucille Lacoste; Jacques Lapointe is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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A specifii inhibitor of glutamyl-tRNA synthetase, analog of glutamyl-adenylate, the Ne-benxoyl-L glutamol AMP, has been synthesized. This compound does not inhibit glutaminyl-tRNA synthetase. Amin~acyl-tRNA synthetases (aaRS) catalyze the esterification of a particular tRNA with its corresponding amino acid. It has been established that this reaction is a two-step event: fit, the activation of the amino acid, and second, the transfer of the activated amino acid to the CCA-end of the cognate tRNA' MS" Amino acid + ATP + aaRS e (aa-AMP) aaRS + PPi @a-AMP) aaRS + tRNA e aa-tRNA+AMP+aaRS Glutamyl-tRNA synthetase (GluRS) has the characteristic, which is common also to the glutaminyl-and arginyl-tRNA synthetase from Ercherichia coli and all other organisms where these synthetases have been studied, of requiring the presence of its cognate tRNA to catalyze the activation of its amino acid substrate? Synthetic analogs of several aminoacyl adenylates ate potent inhibitors of the activation step catalyzed by aaRS.3" With the aim of obtaining a specific inhibitor of GluRS, we have synthesized an analog of glutamyl adenylate and tested its properties in the aminoacylation reaction of tRNAG'" c

Who reads Synthesis of an inhibitor of glutamyl-tRNA synthetase?

Author

Catherine Dorion; Robert Chênevert; Lucille Lacoste; Jacques Lapointe

Publisher

Elsevier Science; Elsevier ; Elsevier Ltd.; Elsevier BV (ISSN 0960-894X)

Published

1993

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)