EC Number   |
Substrates |
Products |
Reversibility |
|---|
    3.5.1.54 | biuret + H2O |
- |
? |
- |
? |
| 3.5.1.54 | malonamic acid + H2O |
- |
? |
- |
? |
| 3.5.1.54 | malonamic acid + hydroxylamine |
hydroxylamine trapping activity |
malonohydroxamate + ? |
- |
? |
| 3.5.1.54 | malonamide + H2O |
- |
? |
- |
? |
| 3.5.1.54 | more |
allophanate also shows nonenzymatic decomposition, half-life at pH 8.0 is 50 h |
? |
- |
? |
| 3.5.1.54 | more |
substrate specificity, no activity with methyl allophanate, hydantoic acid, oxamic acid, hydroxyurea, methyl carbamate, N-methylurea, acetylurea, 1-acetyl-2-thiourea, and semicarbazide, no activity with rhodanine, rhodanine-3-acetic acid, 3-aminorhodanine, (4R)-(-)-2-thioxo-4-thiazolidinecarboxylic acid, (-)-2-oxo-4-thiazolinecarboxylic acid, and 2-amino-5-bromothiazol |
? |
- |
? |
| 3.5.1.54 | more |
allophanate is produced at the active site of the UC C-terminal domain and is translocated to that of the AH N-domain for subsequent reaction. Allophanate is translocated from the active site of UC C-terminal domain to that of the AH N-domain via diffusion through solvent, instead of being channeled through the dimer |
? |
- |
? |
| 3.5.1.54 | more |
the catalytic reaction is catalyzed by either the full-length AtzF or the amidase domain of AtzF, AtzF467. There is no catalytic advantage conferred by the C terminus of AtzF in vitro |
? |
- |
? |
| 3.5.1.54 | more |
binding process of allophanate to allophanate hydrolase, computational analysis, enzyme-substrate interaction, overview |
? |
- |
? |
| 3.5.1.54 | urea-1-carboxylate + H2O |
- |
2 CO2 + 2 NH3 |
- |
? |
