Literature summary extracted from
Michel, C.; Buckel, W.
Coenzyme B12-dependent 2-methylenenglutarate mutase from Clostridium barkeri (1991), FEBS Lett., 281, 108-110.
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
5.4.99.4 |
additional information |
the enzyme is inactivated by light of the wavelength, lambda = 620 nm. Reactivation of up to 50% of the activity is achieved by incubation with coenzyme B12 and dithiothreitol, the substrates 2-methgyleneglutarate or 3-methylitaconate specifically protect the enzyme from inactivation by visible light |
Eubacterium barkeri |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
5.4.99.4 |
Eubacterium barkeri |
- |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
5.4.99.4 |
partial |
Eubacterium barkeri |
Source Tissue
EC Number |
Source Tissue |
Comment |
Organism |
Textmining |
---|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
5.4.99.4 |
2-Methyleneglutarate |
- |
Eubacterium barkeri |
2-Methylene-3-methylsuccinate |
- |
? |
|
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
5.4.99.4 |
vitamin B12 |
dependent on |
Eubacterium barkeri |
|
5.4.99.4 |
vitamin B12 |
during catalysis the Co-C bond of the coenzyme is cleaved |
Eubacterium barkeri |
|