EC Number   |
General Information |
Reference  |
|---|
    6.1.1.1 | physiological function |
CYT-18 also promotes self-splicing of group I intron RNAs by stabilizing the functional structure in the conserved core |
705174 |
| 6.1.1.1 | physiological function |
tyrosyl-tRNA synthetase functions in group I intron splicing |
714246 |
| 6.1.1.1 | more |
dissociating quaternary structures regulating novel functions of other tRNA synthetases |
715585 |
| 6.1.1.1 | physiological function |
although native TyrRS has no known cytokine functions, natural proteolysis of secreted TyrRS releases TyrRSMini, which not only has the same aminoacylation activity as native TyrRS when occuring as a dimer, the monomer is inactive, but TyrRSMini also has strong activity for stimulating migration of polymorphonuclear leukocytes. The migration-stimulating activity is dependent on an ELR tripeptide motif, similar to that in CXC cytokines like IL-8, and also has the familiar bell-shaped concentration dependence seen for CXC cytokines. But TyrRSMini does not induce internalization of CXCR1/2. The TyrRSMini monomer is an agonist, while TyrRSMini dimer is an antagonist of induced PMN cell migration |
715585 |
| 6.1.1.1 | evolution |
phylogenetic relationship of TyrRS sequences, schematic overview |
715934 |
| 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 | 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 | more |
lysine acetylation could be a possible mechanism for modulating aminoacyl-tRNA synthetases enzyme activities, thus affecting translation |
744707 |
| 6.1.1.1 | evolution |
the enzyme belongs to class I of aminoacyl-tRNA synthetases |
-, 744822 |
