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Literature summary extracted from
- Changes in the free energy profile of glutamate mutase imparted by the mutation of an active site arginine residue to lysine (2007), Arch. Biochem. Biophys., 461, 194-199.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 5.4.99.1 | - |
Clostridium cochlearium |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 5.4.99.1 | R100K | mutation significantly impairs the ability of enzyme to catalyze the rearrangement of substrate radical to product radical | Clostridium cochlearium |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.4.99.1 | 0.14 | - |
L-threo-3-methylaspartate | wild-type, pH 7.0 | Clostridium cochlearium |  |
| 5.4.99.1 | 9.5 | - |
L-threo-3-methylaspartate | mutant R100K, pH 7.0 | Clostridium cochlearium | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.4.99.1 | Clostridium cochlearium | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.4.99.1 | L-threo-3-methylaspartate | - |
Clostridium cochlearium | L-glutamate | - |
r | |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.4.99.1 | 0.073 | - |
L-threo-3-methylaspartate | mutant R100K, pH 7.0 | Clostridium cochlearium | |
| 5.4.99.1 | 5.4 | - |
L-threo-3-methylaspartate | wild-type, pH 7.0 | Clostridium cochlearium | |
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Release 2023.1 (January 2023)
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