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Arginyl-tRNA Synthetase from Brewer's Yeast.

Authors :
Thiebe, Rainer
Source :
European Journal of Biochemistry; 2/15/83, Vol. 130 Issue 3, p517-524, 8p
Publication Year :
1983

Abstract

tRNA<superscript>Arg</superscript> and argiuyl-tRNA synthetase have been purified to homogeneity from brewer's yeast by chromatographic methods. Arginyl-tRNA synthetase is a monomeric enzyme with a molecular weight of 72000. Two active forms of the enzyme can be found, they are interconvertible. The more stable conformation is probably the natural one. Arginyl-tRNA synthetase seems to recognize arginine very specifically. No evidence for any proof-reading mechanism could be found. The steady-state mechanism is somewhat different from the types found with arginyl tRNA synthetase from other sources. However, all these results are compatible with a concerted reaction. Simultaneously with the release of AMP or pyrophosphate an allosteric rearrangement occurs. This conversion seems to be determining for the reaction mechanism. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00142956
Volume :
130
Issue :
3
Database :
Complementary Index
Journal :
European Journal of Biochemistry
Publication Type :
Academic Journal
Accession number :
15808277
Full Text :
https://doi.org/10.1111/j.1432-1033.1983.tb07180.x