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Literature summary extracted from
- Role of arg100 in the active site of adenosylcobalamin-dependent glutamate mutase (2004), Biochemistry, 43, 3238-3245.
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 5.4.99.1 | R100K | cob(II)alamin accumulates to a concentration similar to that of the wild-type enzyme, homolysis of the coenzyme is slower by an order of magnitude, compared to wild-type enzyme, glutamate binding is significantly weakened. Mutant does not exhibit the very large deuterium isotope effects that are observed for homolysis of the coenzyme when the wild-type enzyme is reacted with deuterated substrates. Km-value for glutamate is reduced 121fold compared to wild-type enzyme, KM-value for glutamate is increased 17fold compared to wild-type enzyme | Clostridium cochlearium |
| 5.4.99.1 | R100M | no cob(II)alamin detected in UV-visible spectrum. Km-value for glutamate is reduced 276fold compared to wild-type enzyme, KM-value for glutamate is increased 13fold compared to wild-type enzyme | Clostridium cochlearium |
| 5.4.99.1 | R100Y | no cob(II)alamin detected in UV-visible spectrum. Km-value for glutamate is reduced 322fold compared to wild-type enzyme, KM-value for glutamate is increased 17fold compared to wild-type enzyme | Clostridium cochlearium |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.4.99.1 | 0.58 | - |
L-glutamate | 25°C, wild-type enzyme | Clostridium cochlearium |  |
| 5.4.99.1 | 7.6 | - |
L-glutamate | 25°C, mutant enzyme R100Y | Clostridium cochlearium | |
| 5.4.99.1 | 10 | - |
L-glutamate | 25°C, mutant enzyme R100K | Clostridium cochlearium | |
| 5.4.99.1 | 13 | - |
L-glutamate | 25°C, mutant enzyme R100M | 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-glutamate | - |
Clostridium cochlearium | L-threo-3-methylaspartate | - |
? | |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.4.99.1 | 0.0181 | - |
L-glutamate | 25°C, mutant enzyme R100Y | Clostridium cochlearium | |
| 5.4.99.1 | 0.0211 | - |
L-glutamate | 25°C, mutant enzyme R100M | Clostridium cochlearium | |
| 5.4.99.1 | 0.048 | - |
L-glutamate | 25°C, mutant enzyme R100K | Clostridium cochlearium | |
| 5.4.99.1 | 5.8 | - |
L-glutamate | 25°C, wild-type enzyme | Clostridium cochlearium | |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.4.99.1 | adenosylcobalamin | Km-value for wild-type enzyme is 0.005 mM. No cob(II)alamin detected in UV-visible spectrum of mutant enzymes R100M and R100Y. In mutant enzyme R100K cob(II)alamin accumulates to a concentration similar to that of the wild-type enzyme, homolysis of the coenzyme is slower by an order of magnitude, compared to wild-type enzyme. Mutant does not exhibit the very large deuterium isotope effects that are observed for homolysis of the coenzyme when the wild-type enzyme is reacted with deuterated substrates | Clostridium cochlearium | |
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