EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
5.4.99.1 | Clostridium cochlearium | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
5.4.99.1 | L-threo-3-methylaspartate = L-glutamate | radical mechanism of the conversion of glutamate to methylaspartate catalyzed by glutamate mutase by quantum mechanical/molecular mechanical simulations based on density functional theory, crystal structure analysis | Clostridium cochlearium |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.4.99.1 | L-threo-3-methylaspartate | - |
Clostridium cochlearium | L-glutamate | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
5.4.99.1 | Glutamate mutase | - |
Clostridium cochlearium |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
5.4.99.1 | adenosylcobalamin | dependent on, binding structure, modeling, overview | Clostridium cochlearium |
EC Number | General Information | Comment | Organism |
---|---|---|---|
5.4.99.1 | additional information | residue Glu117 and the arginine claw have a strong influence, and also residues Glu 214, Lys 322, Gln 147, Glu 330, Lys 326, and Met 294 play a catalytic role. The arginine claw keeps the intermediates in place and is probably responsible for the enantioselectivity. Glu 171 temporarily accepts a proton from the glutamyl radical intermediate and donates it back at the end of the reaction | Clostridium cochlearium |