EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
6.1.1.3 | mitochondrion | - |
Saccharomyces cerevisiae | 5739 | - |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
6.1.1.3 | Mg2+ | required | Saccharomyces cerevisiae |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.1.1.3 | ATP + L-threonine + tRNAThr | Saccharomyces cerevisiae | - |
AMP + diphosphate + L-threonyl-tRNAThr | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
6.1.1.3 | Saccharomyces cerevisiae | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
6.1.1.3 | ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr | reaction mechanism and structure-function relationship, modeling, overview | Saccharomyces cerevisiae |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.1.1.3 | ATP + L-threonine + tRNAThr | - |
Saccharomyces cerevisiae | AMP + diphosphate + L-threonyl-tRNAThr | - |
? | |
6.1.1.3 | additional information | residues Gln180 and Gln292 are important in cofactor binding | Saccharomyces cerevisiae | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
6.1.1.3 | Mst1 | - |
Saccharomyces cerevisiae |
6.1.1.3 | Threonyl-tRNA synthetase | - |
Saccharomyces cerevisiae |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
6.1.1.3 | ATP | - |
Saccharomyces cerevisiae |
EC Number | General Information | Comment | Organism |
---|---|---|---|
6.1.1.3 | additional information | analysis of pre-transfer editing mechanism in yeast mitochondrial threonyl-tRNA synthetase (MST1) via the combined application of classical molecular dynamics and QM/MM-MD free energy calculations. The X-ray crystal structure of a single monomer of MST1 from Saccharomyces cerevisiae, PDB ID 3UH0 at 2.0 A resolution, is used as the starting structure for the computational studies. Molecular dynamics simulations, overview. Residues Gln180 and Gln292 are important in cofactor binding, Gln180 and Gln292 do not alternate in their H bonding to the Ser-AMP phosphate. Water molecules are able to enter and replace the H bonding networks and, as a result, MST1-bound Ser-AMP has increased variability in its positioning within the active site in comparison to Thr-AMP. A H-bond is intermittently formed between the alpha-amino group of the Thr and Ser and the side chain hydroxyl of Tyr270, though with markedly greater occurrence for Thr-AMP (22%) in comparison to Ser-AMP (7%). Mechanism of Thr-AMP and Ser-AMP hydrolysis determination by umbrella sampling on both ligands from three different initial conformations | Saccharomyces cerevisiae |
6.1.1.3 | physiological function | aminoacyl-tRNA synthetases (aaRSs) catalyze the activation of the corresponding amino acids and attachment to their cognate tRNAs with extremely high fidelity due to pre- and post-transfer editing processes | Saccharomyces cerevisiae |