Phenylalanyl‐tRNA synthetase from Thermus thermophilus can attach two molecules of phenylalanine to tRNAPhe
- 26 October 1992
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 311 (3) , 192-194
- https://doi.org/10.1016/0014-5793(92)81099-8
Abstract
Phenylalanyl-tRNA synthetase from the extreme thermophilic bacterium Thermus thermophilus can incorporate more than one molecule of phenylalanine into the tRNAPhe. It is shown that the ‘hyperaminoncylated’ tRNAPPhe is the bis-2′,3′-O-phenylalanyl-tRNAPhe, and its formation is typical for the thermophilic enzyme but does not occur for E. coli phenylalanyl-tRNA synthetase under the same conditions.Keywords
This publication has 9 references indexed in Scilit:
- Stereoselective formation of bis(α-aminoacyl) esters of 5′-AMP suggests a primitive peptide synthesizing system with a preference for l-amino acidsPublished by Elsevier ,2003
- Sequence and base modifications of two phenylalanine-tRNAs from Thermus thermophilus HB8Nucleic Acids Research, 1992
- Phenylalanyl‐tRNA synthetase from Thermus thermophilus HB8 Purification and properties of the crystallizing enzymeFEBS Letters, 1988
- Purification and Thermal Stability of Several Amino Acid-Specific tRNAs from an Extreme Thermophile, Thermus thermophilus HB8The Journal of Biochemistry, 1980
- On dealing with anomalies in the transfer RNA aminoacylation reaction in partially purified systemsArchives of Biochemistry and Biophysics, 1977
- Isoleucyl-tRNA synthetase inactivation and the extent of aminoacylation of tRNAIle from Escherichia coliBiochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1977
- Studies towards the complete sequence determination of proteins by mass spectrometry: Derivatisation of methionine, cysteine and arginine containing peptidesBiochemical and Biophysical Research Communications, 1973
- Interpretation of Incomplete Reactions in tRNA AminoacylationEuropean Journal of Biochemistry, 1972
- Studies on methionyl-tRNA synthetase III. Enzyme dependence for maximum methionyl-tRNA formationBiochimica et Biophysica Acta (BBA) - Enzymology, 1968