EC Number   |
Reaction |
Reference |
|---|
    6.1.1.1 | ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr |
- |
- |
| 6.1.1.1 | ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr |
amino acid residues Y37 and Q195 are involved in substrate specificity determination |
653691 |
| 6.1.1.1 | ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr |
functional importance of Ser200 in the catalytic domain in line with an involvement of A73 rather than N1-N72 in tyrosine identity, active site structure, role of clusters 1 and 2 in tRNATyr acceptor arm |
677165 |
| 6.1.1.1 | ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr |
mechanism |
650300, 653786 |
| 6.1.1.1 | ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr |
mechanism, class I enzyme has a class II mode of cognate tRNA recognition |
-, 650993 |
| 6.1.1.1 | ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr |
mechanism, residues Asp78, Tyr169, Gln173, Asp194, and Gln195 are involved in catalysis |
652832 |
| 6.1.1.1 | ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr |
molecular dynamics simulations of TyrRS in its free form and complexed with Tyr, ATP, tyrosyl adenylate and inhibitor respectively are carried out to investigate the ligand-linked conformational stability changes associated with its catalytic cycle. Unliganded TyrRS samples a more relaxed conformational space than substrate-bound TyrRS. There are three high flexibility regions encompassing residues 114-118, 128-133, and 226-238 respectively. The region which includes the KFGKS motif shows the highest difference in fluctuations |
692144 |
| 6.1.1.1 | ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr |
reaction via reactive aminoacyl-adenylate intermediate, anticodon recognition mode and involved residues Tyr43, Asp177, Tyr170, Gln174 and Gln192, overview, the lack of cross-reactivity between archaeal/eukaryotic and bacterial TyrRS-tRNATyr pairs most probably lies in the different sequence of the last base pair of the acceptor stem, C1-G72 vs G1-C72, of tRNATyr |
676225 |
| 6.1.1.1 | ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr |
S224 and S226 are involved in the catalytic mechanism, the sequence 222KKSSS226, termed KMSSS motif, stabilizes the the transition state for the tyrosine activation reactionby interacting with the diphosphate moiety of ATP |
652281 |
| 6.1.1.1 | ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr |
S356 and K395 play key roles in tRNA binding, H306, a residue at the junction of the catalytic and tRNA binding domains, stabilizes the Tyr-AMP:enzyme complex |
651278 |
