Open AccessYeast Phenylalanyl‐tRNA Synthetase
Author(s) -
FASIOLO Franco,
EBEL JeanPierre
Publication year - 1974
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1974.tb03830.x
Subject(s) - adenylate kinase , ternary complex , transfer rna , phenylalanine , enzyme , chemistry , stereochemistry , biochemistry , amino acid , rna , gene
Phenylalanyl‐tRNA synthetase from yeast forms an enzyme · phenylalanyl adenylate complex, which has been isolated from the reaction mixture by gel filtration. The study of this complex leads to the conclusion that there are two binding sites for phenylalanyl adenylate per molecule of enzyme. No complex between enzyme and ATP could be characterised. Mg 2+ is required for complex formation, but it can be replaced by monovalent cations in the transfer of phenylalanine from the complex to tRNA Phe . The kinetics of the transfer reaction show evidence that the rate‐limiting step is not the release of enzyme‐bound Phe‐tRNA Phe , but the acylation of tRNA Phe after the ternary complex phenylalanyl adenylate · enzyme · tRNA Phe has been formed.