Proteolytic cleavage of methionyl transfer ribonucleic acid synthetase from Bacillus stearothermophilus: effects on activity and structure
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00557a012
Reference48 articles.
1. The Mechanism of Reaction of Methionyl-tRNA Synthetase from Escherichia coli. Interaction of the Enzyme with Ligands of the Amino-Acid-Activation Reaction
2. The Mechanism of Action of Methionyl-tRNA Synthetase from Escherichia coli. 1. Fluorescence Studies on tRNAMet Binding as a Function of Ligands, Ions and pH
3. The Mechanism of Action of Methionyl-tRNA Synthetase from Escherichia coli. Mechanism of the Amino-Acid Activation Reaction Catalyzed by the Native and the Trypsin-Modified Enzymes
4. The amino acid activation reaction catalyzed by methionyl-transfer RNA synthetase: Evidence for synergistic coupling between the sites for methionine adenosine and pyrophosphate
5. The Mechanism of Action of Methionyl-tRNA Synthetase from Escherichia coli. Inhibition by Adenosine and 8-Aminoadenosine of the Amino-Acid Activation Reaction
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