Arginyl‐tRNA Synthetase from Brewer's Yeast

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Abstract
TRNAArg and arginyl-tRNA synthetase were purified to homogeneity from brewer''s yeast by chromatographic methods. Arginyl-tRNA synthetase is a monomeric enzyme with a MW of 72,000. 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. These results are compatible with a concerted reaction. Simultaneously with the release of AMP or PPi an allosteric rearrangement occurs. This conversion seems to be determining for the reaction mechanism.