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Literature summary extracted from
- Theoretical analysis of the diradical nature of adenosylcobalamin cofactor-tyrosine complex in B12-dependent mutases: inspiring PCET-driven enzymatic catalysis (2010), J. Phys. Chem. B, 114, 5928-5939.
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.4.99.1 | Clostridium cochlearium | P80077 | methylaspartate mutase E chain (subunit epsilon) | - |
| 5.4.99.1 | Clostridium cochlearium | P80078 | methylaspartate mutase S chain (subunit sigma) | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.4.99.1 | L-Glu | - |
Clostridium cochlearium | L-threo-3-methylaspartate | - |
r |  |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.4.99.1 | Glm | - |
Clostridium cochlearium |
| 5.4.99.1 | Glutamate mutase | - |
Clostridium cochlearium |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.4.99.1 | adenosylcobalamin | - |
Clostridium cochlearium | |
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Release 2023.1 (January 2023)
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