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The non-proteinogenic amino acids m-fluorotyrosine and 2,4-dihydroxyphenylalanine demonstrated a respective 6- and 12-fold greater binding affinity to the purified tyrosyl-tRNA synthetase from Escherichia coli than that from human cytosol. The… Click to show full abstract
The non-proteinogenic amino acids m-fluorotyrosine and 2,4-dihydroxyphenylalanine demonstrated a respective 6- and 12-fold greater binding affinity to the purified tyrosyl-tRNA synthetase from Escherichia coli than that from human cytosol. The differential binding was identified by probing the substrate selectivity of the two enzymes with structural analogues of tyrosine using a thermodynamic technique.
Keywords:
thermodynamic analysis;
synthetases revealed;
analysis tyrosyl;
revealed bacterial;
tyrosyl trna;
trna synthetases
Journal Title: Australian Journal of Chemistry
Year Published: 2021
Link to full text (if available)
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Journal Title: Australian Journal of Chemistry
Year Published: 2021
Link to full text (if available)
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recommendations!