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Literature summary extracted from
- Electron-nuclear double resonance spectroscopy investigation of 4-hydroxybutyryl-CoA dehydratase from Clostridium aminobutyricum: Comparison with other flavin radical enzymes (1997), Biol. Chem., 378, 843-849.
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.2.1.120 | Clostridium aminobutyricum | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.2.1.120 | 4-hydroxybutanoyl-CoA | reaction involves cleavage of an unactivated C-H bond at the beta-carbon | Clostridium aminobutyricum | but-3-enoyl-CoA + H2O | - |
r |  |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.1.120 | 4Fe-4S-center | - |
Clostridium aminobutyricum | |
| 4.2.1.120 | FAD | substrate interacts with the flavin. Partial reduction of the enzyme using dithionite results in formation of a neutral flavin semiquinone, which may interact with the 4Fe-4S-center | Clostridium aminobutyricum | |
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Release 2023.1 (January 2023)
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