Crystallization (Comment) | Organism |
---|---|
crystals of purified free enzyme and enzyme complexed with L-methionine are diffused by several methionine analogues, i.e. L-difluoromethionine, L-trifluoromethionine, D,L-phosphomethionine and D,L-iodo-methionine, X-ray diffraction structure determination at 1.9 A resolution and analysis | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-methionine + tRNAMet | Escherichia coli | - |
AMP + diphosphate + L-methionyl-tRNAMet | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P00959 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
ATP + L-methionine + tRNAMet = AMP + diphosphate + L-methionyl-tRNAMet | substrate binding and mechanism | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-methionine + tRNAMet | - |
Escherichia coli | AMP + diphosphate + L-methionyl-tRNAMet | - |
? | |
ATP + L-methionine + tRNAMet | binding of L-methionine induces conformational changes of the active site of the enzyme, amino acid residues Y15 and W253 are important for the strength of binding, H301 is responsible for the specific recognition of the sulfur atom of methionine | Escherichia coli | AMP + diphosphate + L-methionyl-tRNAMet | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Methionine translase | - |
Escherichia coli |
Methionine--tRNA ligase | - |
Escherichia coli |
Methionyl tRNA synthetase | - |
Escherichia coli |
Methionyl-transfer ribonucleate synthetase | - |
Escherichia coli |
Methionyl-transfer ribonucleic acid synthetase | - |
Escherichia coli |
Methionyl-transfer RNA synthetase | - |
Escherichia coli |
MetRS | - |
Escherichia coli |
Synthetase, methionyl-transfer ribonucleate | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Escherichia coli |