6.1.1.1	evolution	analysis of evolutionary conservation of KMSKS motif in tyrosyl-tRNA synthetases, YRSs, two YRSs of Pyrococcus horikoshii and Leishmania major have an overall root mean squared deviation calculated as 3.2 A, although the primary sequences for ATP recognition motifs in Pyrococcus horikoshii and Leishmania major YRSs are identical (KMSKS). The KMSKS loop in YRSs is evolutionarily conserved and mediates inter-molecular interactions between YRS and ATP, Conformational landscape of KMSKS loops in YRSs, overview	-, 745655	
6.1.1.1	evolution	domain organization of TyrRS from eukaryotes and prokaryotes, overview	-, 745348	
6.1.1.1	evolution	mammalian TyrRS has evolved to be significantly less accurate than its bacterial counterpart. Different evolutionary constraints determine the accuracy of translation quality control in eukaryotes and bacteria. Functional comparisons of mammalian and bacterial tyrosyl-tRNA synthetase reveal key differences at residues responsible for amino acid recognition, highlighting differences in evolutionary constraints for translation quality control, overview	745300	
6.1.1.1	evolution	phylogenetic relationship of TyrRS sequences, schematic overview	715934	
6.1.1.1	evolution	the enzyme belongs to class I of aminoacyl-tRNA synthetases	-, 744822	
6.1.1.1	evolution	the enzyme belongs to the class I aminoacyl-tRNA synthetase family	-, 745576	
6.1.1.1	evolution	TyrRS belongs to the class I aminoacyl-tRNA synthetases (aaRSs), Evolutionary analysis of SerRS and TyrRS, overview	746475	
6.1.1.1	evolution	TyrRS is a member of class I aminoacyl-tRNA synthetases	744707	
6.1.1.1	malfunction	lysine acetylation can be a possible mechanism for modulating aminoacyl-tRNA synthetases enzyme activities, thus affecting translation. Of recombinantly expressed site-specifically acetylated TyrRS variants, TyrRS-85AcK and -235AcK show dramatic decreases in activity. Variant TyrRS-238AcK has no detectable activity, while variants TyrRS-144AcK and -355AcK have similar activities compared to the wild-type TyrRS. TyrRS-85AcK has a fivefold increase in the KM value for ATP, indicating its role in ATP binding. TyrRS-235AcK has slightly changed KM values for both ATP and tyrosine but a 200fold decrease in catalytic efficiency, suggesting its role in catalysis. K235 and K238 of TyrRS characterized in this study are the two lysine residues in the KMSKS motif. Kinetics for acetylated mutant variants, overview	744707	
6.1.1.1	malfunction	of six mutants tested, two are active towards D-Tyr; one of these has an inverted stereospecificity, with a large preference for D-Tyr, but its activity is low	746405