EC Number | Crystallization (Comment) | Organism |
---|---|---|
6.1.1.10 | purified enzyme complexed with L-methionine, protein solution: 8 mg/ml protein, 10 mM KH2PO4, pH 7.3, 10 mM 2-mercaptoethanol, initiating by microseeding with crystals from the free enzyme at 20°C, in 1.1 ammonium citrate, 0.5% v/v methyl-2,4-pentanediol, 0.6 mM L-methionine, 2 mM 2-mercaptoethanol, 30 mM phosphate buffer, pH 7.0, 1 day, X-ray diffraction structure determination at 1.8 A resolution, structure analysis and modeling | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.1.1.10 | ATP + L-methionine + tRNAMet | Escherichia coli | - |
AMP + diphosphate + L-methionyl-tRNAMet | - |
? | |
6.1.1.10 | additional information | Escherichia coli | L-homocysteine is a natural competitor to L-methionine, its activation by the enzyme is prevented by a proof-reading mechanism, structural requirements are determined form the crystal structure | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
6.1.1.10 | Escherichia coli | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
6.1.1.10 | ATP + L-methionine + tRNAMet = AMP + diphosphate + L-methionyl-tRNAMet | substrate recognition, editing, binding and reaction mechanism | Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.1.1.10 | ATP + L-methionine + tRNAMet | - |
Escherichia coli | AMP + diphosphate + L-methionyl-tRNAMet | - |
? | |
6.1.1.10 | ATP + L-methionine + tRNAMet | substrate editing mechanism, L-methionine is bound to a hydrophobic pocket formed by amino acid residues W253, Y15, A256, P257, L13, A12, I297, Y260, H301, and W305 around the side-chain | Escherichia coli | AMP + diphosphate + L-methionyl-tRNAMet | - |
? | |
6.1.1.10 | additional information | L-homocysteine is a natural competitor to L-methionine, its activation by the enzyme is prevented by a proof-reading mechanism, structural requirements are determined form the crystal structure | Escherichia coli | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
6.1.1.10 | Methionine translase | - |
Escherichia coli |
6.1.1.10 | Methionine--tRNA ligase | - |
Escherichia coli |
6.1.1.10 | Methionyl tRNA synthetase | - |
Escherichia coli |
6.1.1.10 | Methionyl-transfer ribonucleate synthetase | - |
Escherichia coli |
6.1.1.10 | Methionyl-transfer ribonucleic acid synthetase | - |
Escherichia coli |
6.1.1.10 | Methionyl-transfer RNA synthetase | - |
Escherichia coli |
6.1.1.10 | MetRS | - |
Escherichia coli |
6.1.1.10 | Synthetase, methionyl-transfer ribonucleate | - |
Escherichia coli |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
6.1.1.10 | ATP | - |
Escherichia coli |