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Literature summary for 2.1.2.5 extracted from
- Monofunctional domains of formiminotransferase-cyclodeaminase retain similar conformational stabilities outside the bifunctional octamer (1997), Biochim. Biophys. Acta, 1338, 223-232.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Urea | - |
Sus scrofa |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Sus scrofa | - |
- |
- |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | transferase domain is expressed in Escherichia coli as monofunctional dimer | Sus scrofa |
| homooctamer | each identical subunit of octameric bifunctional formiminotransferase cyclodeaminase consists of a transferase and a deaminase domain connected by a short linker sequence | Sus scrofa |
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