Methionyl‐tRNA Synthetase from Escherichia coli
- 1 May 1979
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 96 (1), 87-92
- https://doi.org/10.1111/j.1432-1033.1979.tb13016.x
Abstract
Both the aminoacylation and isotopic ATP-PPi exchange activities of native and trypsin-modified methionyl-tRNA synthetases from E. coli are specifically inactivated by incubation in the presence of periodate-treated initiator tRNAMet. The inactivation proceeds through the formation of a reversible Schiff''s base between the .epsilon.-amino group of a lysine within the catalytic center of the enzyme and the 2'',3''-aldehyde groups created at the 3''-terminal ribose of tRNA. The Schiff''s base may be stabilized by reduction with NaBH4. Intact .**GRAPHIC**. competes with the inactivation by its dialdehyde. It was verified in the case of the modified enzyme that the protection is afforded according to an equilibrium constant identical to that for .**GRAPHIC**. binding at the active site of the enzyme. The incorporation of 1 molecule of the dialdehyde of [14C]tRNA completely destroys the activity of the monomeric trypsin-modified methionyl-tRNA synthetase.This publication has 19 references indexed in Scilit:
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