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Literature summary extracted from
- On the role of two different cobalt(II) species in coenzyme B12-dependent 2-methyleneglutarate mutase from Clostridium barkeri (1993), Biol. Chem. Hoppe-Seyler, 374, 85-90.
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.4.99.4 | Itaconate | competitive | 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 | - |
Eubacterium barkeri |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 5.4.99.4 | 2-Methyleneglutarate = 2-methylene-3-methylsuccinate | formation of an unusual oxygen-sensitive Co(II) species during catalysis | Eubacterium barkeri |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.4 | additional information | - |
- |
Eubacterium barkeri |
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 | cobamide | the enzyme contains adenosylcobalamin and varying amounts of oxygen-stable cob(II)alamin. The content of total cobalamin is 2-4 mol/ml enzyme, the content of cob(II)alamin is 6-11% of the total cobalamin. The oxygen-stable cob(II)alamin is not involved in catalysis | Eubacterium barkeri | |
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