Organism | UniProt | Comment | Textmining |
---|---|---|---|
Clostridium cochlearium | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
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 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-threo-3-methylaspartate | - |
Clostridium cochlearium | L-glutamate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Glutamate mutase | - |
Clostridium cochlearium |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
adenosylcobalamin | dependent on, binding structure, modeling, overview | Clostridium cochlearium |
General Information | Comment | Organism |
---|---|---|
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 |