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Structure and Function of Transfer Ribonucleic Acid

II. ENZYME-SUBSTRATE COMPLEXES WITH VALYL RIBONUCLEIC ACID SYNTHETASE FROM YEAST

Ulf Lagerkvist 1, Lars Rymo 1, and Johan Waldenström 1

From the 1 From the Department of Medical Biochemistry, University of Gothenburg, Gothenburg, Sweden

When valyl ribonucleic acid synthetase of yeast was incubated with valine, adenosine triphosphate, and Mg++, an enzyme-AMP-valyl complex was formed that could transfer its amino acid residue to transfer RNA (tRNA) in a reversible reaction that did not require Mg++. The enzyme also formed a specific complex with tRNA of yeast specific for valine, but not with tRNA of Escherichia coli specific for valine. No complex formation was obtained with tRNAs specific for amino acids other than valine. Complex formation required an intact 3'-hydroxyl end group, as judged by the absence of competitive inhibition with periodate-oxidated tRNA or tRNA stripped of its terminal adenosine.

Submitted on May 9, 1966


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Copyright © 1966 by the American Society for Biochemistry and Molecular Biology.
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