Open AccessSome Properties of Lysyl Ribonucleic Acid Synthetase from Escherichia coli
Author(s) -
Waldenström J.
Publication year - 1968
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1968.tb00363.x
Subject(s) - escherichia coli , lysine , yeast , biochemistry , enzyme , sephadex , rna , substrate (aquarium) , chemistry , amino acid , biology , gene , ecology
When the lysyl‐RNA synthetase from Escherichia coli was incubated with ATP and L‐lysine in the presence of Mg ++ , a complex of lysyl‐RNA synthetase, AMP and lysine was formed. The complex was isolated by filtration on Sephadex G‐25. Maximum complex formation was obtained at a molar ratio of substrate to enzyme between 3 and 4. The complex was very stable at low temperatures in the absence of Mg ++ , while incubation at 45° for 10 minutes gave 75% breakdown of the complex. The amino acid of the complex could be transferred to transferRNA in a reversible reaction that did not require Mg ++ . The transfer reaction was enhanced by the monovalent cations NH 4 + , Na + , and K + . The lysyl‐RNA synthetase from E. coli recognized about 70% of the lysine specific chains of yeast transferRNA, while the yeast enzyme recognized about 80% of the lysine specific chains of E. coli transferRNA. The esterification of E. coli transferRNA by the yeast enzyme proceeded at only 2% of the rate obtained with homologous transferRNA, while the E. coli enzyme esterified yeast transferRNA at about 60% of the rate obtained with E. coli transferRNA.