The Aminoacyl Transfer Ribonucleic Acid Synthetases

Rat liver threonyl-transfer RNA synthetase forms an ATP-enzyme complex when incubated with ATP and magnesium ions. The formation, stability, and reactivity of the complex have been studied. Enzyme-bound ATP serves as substrate in the over-all reaction of threonyl-tRNA formation at concentration leve...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of biological chemistry 1970-01, Vol.245 (1), p.93-101
Main Authors: Allende, Catherine C., Chaimovich, Hernán, Gatica, Marta, Allende, Jorge E.
Format: Article
Language:English
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Rat liver threonyl-transfer RNA synthetase forms an ATP-enzyme complex when incubated with ATP and magnesium ions. The formation, stability, and reactivity of the complex have been studied. Enzyme-bound ATP serves as substrate in the over-all reaction of threonyl-tRNA formation at concentration levels at which free ATP and enzyme do not give rise to product. Threonine-specific tRNA has a labilizing effect on the complex. The initial velocity of the over-all reaction has been studied. The nature of the kinetic patterns obtained shows that the reaction is bi uni uni bi ping pong. The kinetic evidence also indicates that ATP interacts with the threonyl-tRNA synthetase as the first substrate in the reaction sequence shown: [see PDF for equation]
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)63426-X