The amino acid sequence of the tyrosyl-tRNA synthetase from Bacillus stearothermophilus.Winter G., Koch G.L.E., Hartley B.S., Barker D.G.View abstractCited forNUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-124; 136-157 AND 172-419CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCEur. J. Biochem. 132:383-387 (1983)Cited in1
A transcription terminator in the 5' non-coding region of the tyrosyl tRNA synthetase gene from Bacillus stearothermophilus.Waye M.M.Y., Winter G.View abstractCited forNUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCEur. J. Biochem. 158:505-510 (1986)Cited in11
Deletion mutagenesis using an 'M13 splint': the N-terminal structural domain of tyrosyl-tRNA synthetase (B. stearothermophilus) catalyses the formation of tyrosyl adenylate.Waye M.M.Y., Winter G., Wilkinson A.J., Fersht A.R.View abstractCited forFUNCTION, BIOPHYSICOCHEMICAL PROPERTIESCategoriesFunctionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCEMBO J. 2:1827-1829 (1983)Cited in1
Construction of heterodimer tyrosyl-tRNA synthetase shows tRNATyr interacts with both subunits.Carter P., Bedouelle H., Winter G.View abstractCited forINTERACTION WITH TRNA(TYR), SUBUNITCategoriesInteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCProc. Natl. Acad. Sci. U.S.A. 83:1189-1192 (1986)Cited in1
Role of residue Glu152 in the discrimination between transfer RNAs by tyrosyl-tRNA synthetase from Bacillus stearothermophilus.Vidal-Cros A., Bedouelle H.View abstractCited forFUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-45; GLU-152; THR-224; LYS-410 AND LYS-411CategoriesFunction, Phenotypes & VariantsSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Mol. Biol. 223:801-810 (1992)Cited in1
The 'KMSKS' motif in tyrosyl-tRNA synthetase participates in the initial binding of tRNA(Tyr).Xin Y., Li W., First E.A.View abstractCited forFUNCTION, CATALYTIC ACTIVITY, MOTIF, MUTAGENESIS OF LYS-230; PHE-231; GLY-232; LYS-233 AND THR-234CategoriesFunction, Family & Domains, Phenotypes & VariantsSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCBiochemistry 39:340-347 (2000)Cited in1
Correlating amino acid conservation with function in tyrosyl-tRNA synthetase.Xin Y., Li W., Dwyer D.S., First E.A.View abstractCited forFUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF THR-40; HIS-45; HIS-48; LYS-82 AND ARG-86CategoriesFunction, Phenotypes & VariantsSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Mol. Biol. 303:287-298 (2000)Cited in1
Stabilization of the transition state for the transfer of tyrosine to tRNA(Tyr) by tyrosyl-tRNA synthetase.Xin Y., Li W., First E.A.View abstractCited forFUNCTION, CATALYTIC ACTIVITY, MOTIF, MUTAGENESIS OF ASP-78; TYR-169; GLN-173; ASP-194 AND GLN-195CategoriesFunction, Family & Domains, Phenotypes & VariantsSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Mol. Biol. 303:299-310 (2000)Cited in1
An essential residue in the flexible peptide linking the two idiosynchratic domains of bacterial tyrosyl-tRNA synthetases.Gaillard C., Bedouelle H.View abstractCited forFUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LEU-322; PHE-323; SER-324; GLY-325 AND PHE-339CategoriesFunction, Phenotypes & VariantsSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCBiochemistry 40:7192-7199 (2001)Cited in1
Tyrosyl-tRNA synthetase forms a mononucleotide-binding fold.Bhat T.N., Blow D.M., Brick P., Nyborg J.Cited forX-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS)CategoriesStructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Mol. Biol. 158:699-709 (1982)Cited in1
Structure of tyrosyl-tRNA synthetase refined at 2.3-A resolution. Interaction of the enzyme with the tyrosyl adenylate intermediate.Brick P., Bhat T.N., Blow D.M.View abstractCited forX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH TYROSINECategoriesInteraction, StructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Mol. Biol. 208:83-98 (1989)Cited in1