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Literature summary for 5.4.99.4 extracted from
- Coenzyme B12-dependent 2-methylenenglutarate mutase from Clostridium barkeri (1991), FEBS Lett., 281, 108-110.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 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
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Eubacterium barkeri | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| partial | Eubacterium barkeri |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2-Methyleneglutarate | - |
Eubacterium barkeri | 2-Methylene-3-methylsuccinate | - |
? |  |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| vitamin B12 | dependent on | Eubacterium barkeri | |
| vitamin B12 | during catalysis the Co-C bond of the coenzyme is cleaved | Eubacterium barkeri | |
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Release 2023.1 (January 2023)
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