EC Number   |
General Information |
Reference |
|---|
    6.1.1.1 | malfunction |
reduced amino acid specificity of mammalian tyrosyl-tRNA synthetase is associated with elevated mistranslation of Tyr codons. Mischarging of tRNATyr with noncognate Phe by tyrosyl-tRNA synthetase is responsible for mistranslation. Steady-state kinetic analyses of CHO cytoplasmic tyrosyl-tRNA synthetase reveals a 25fold lower specificity for Tyr over Phe as compared with previously characterized bacterial enzymes, consistent with the observed increase in translation error rates during tyrosine limitation |
745300 |
| 6.1.1.1 | more |
dissociating quaternary structures regulating novel functions of other tRNA synthetases |
715585 |
| 6.1.1.1 | more |
enzyme MtTyrRS contains the HIGH-like and KFGKS catalytic motifs that catalyze amino acid activation with ATP.The conformational mobility of MtTyrRS catalytic KFGKS loop is analyzed by 100-ns all-atoms molecular dynamics simulations of the free enzyme and its complexes with different substrates: tyrosine, ATP, and the tyrosyl-adenylate intermediate. In the closed state of the active site, the KFGKS loop, readily adopts different stable conformations depending on the type of bound substrate. The closed state of the loop is stabilized by dynamic formation of two antiparallel beta-sheets at flanking ends which hold the KFGKS fragment inside the active center. Molecular dynamics simulations, conformation of the MtTyrRS catalytic loop in substrate?bound states, detailed overview |
-, 744822 |
| 6.1.1.1 | more |
lysine acetylation could be a possible mechanism for modulating aminoacyl-tRNA synthetases enzyme activities, thus affecting translation |
744707 |
| 6.1.1.1 | more |
molecular dynamics modeling of substrates L- and D-Tyr into the active site of wild-type enzyme and mutants D81R and E36Q using the PDB ID 1J1U X-ray structure, superimposed based on their protein/tRNA environment, enzyme molecular dynamics simulation amd modeling, structure-function analysis, detailed overview |
-, 745576 |
| 6.1.1.1 | more |
residues, not conserved between bacteria and eukaryotes, Cys35, His48, Thr51, and Lys233 in bacterial TyrRS interact with ATP during transition state formation. Comparison the Geobacillus stearothermophilus, PDB ID 1tyd, and human, PDB ID 1q11, TyrRS active sites, overview. Hydrogen-bonding interactions between bacterial TyrRS residues Asp176 and Tyr34 and the substrate Tyr hydroxyl group help confer amino acid specificity to the enzyme |
745300 |
| 6.1.1.1 | more |
the LdTyrRS polypeptide chain consists of two pseudo-monomers, each consisting of two domains. Comparing the two independent chains in the asymmetric unit reveals that the two pseudo-monomers of LdTyrRS can bend with respect to each other essentially as rigid bodies. This flexibility might be useful in the positioning of tRNA for catalysis since both pseudo-monomers in the LdTyrRS chain are needed for charging tRNATyr. The LdTyrRS active site contains two critical pockets: the tyrosine binding pocket (YBP) where the tyrosyl group of inhibitor TyrSA is situated, and the adenine binding pocket (ABP) where the adenine moiety of TyrSA binds. Residues making hydrogen bonds with the TyrSA tyrosyl group in the tyrosine binding pocket (YBP) are Y36, Y163, Q167, D170 and Q185. Residues G38, A72 and F75 are responsible for the hydrophobic interactions between enzyme and tyrosine moiety in the YBP. An extra pocket (EP) appears to be present near the adenine binding. The extra pocket appears to be present near the adenine binding region of LdTyrRS, this pocket is absent in the two human homologous enzymes. Structure-based modelling, overview |
744442 |
| 6.1.1.1 | more |
the TyrRS stereospecificity is robust towards charge rearrangements near the ligand. Whereas most aminoacyl-tRNA synthetases (aaRSs) have a strong preference for their L-amino acid substrate, TyrRS has a detectable, natural activity for the D-tyrosine stereoisomer, only tenfold less than for L-Tyr; additional protection against D-Tyr is usually provided by another enzyme, D-aminoacyl-tRNA hydrolase. Enzyme molecular dynamics simulations using the crystal structure of Escherichia coli TyrRS bound to a tyrosyl adenylate analogue, PDB ID 1VBM |
746405 |
| 6.1.1.1 | more |
tyrosyl-tRNA synthetase structure comparisons, the KMSKS loop is very variable in conformation, intrinsic conformational heterogeneity in KMSKS loop that is independent of occupancy of active site. Differential centroid distance analyses between KMSKS motif and Rossmann fold domain reveal an intriguing bimodal distribution. The KMSKS loop is positioned at the intersection of Rossmann fold and the C-terminal region and plays a role in ATP binding and catalysis. KMSKS loop orientation and conformation can be independent of ATP binding, conformational flexibility of KMSKS loop, overview |
-, 745655 |
| 6.1.1.1 | more |
tyrosyl-tRNA synthetase structure comparisons, the KMSKS loop uĆs very variable in conformation, intrinsic conformational heterogeneity in KMSKS loop that is independent of occupancy of active site. Differential centroid distance analyses between KMSKS motif and Rossmann fold domain reveal an intriguing bimodal distribution. The KMSKS loop is positioned at the intersection of Rossmann fold and the C-terminal region and plays a role in ATP binding and catalysis. KMSKS loop orientation and conformation can be independent of ATP binding, conformational flexibility of KMSKS loop, overview |
745655 |
