CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.630 | Aminopeptidase |
|
3.40.630.10 | Zn peptidases |
Domain Context
CATH Clusters
| Superfamily | Zn peptidases |
| Functional Family | Allantoate amidohydrolase |
Enzyme Information
| 3.5.1.87 |
N-carbamoyl-L-amino-acid hydrolase.
based on mapping to UniProt Q53389
N-carbamoyl-L-2-amino acid (a 2-ureido carboxylate) + H(2)O = L-2-amino acid + NH(3) + CO(2).
-!- This enzyme, along with EC 3.5.1.77, EC 5.1.99.5 and EC 3.5.2.2, forms part of the reaction cascade known as the 'hydantoinase process', which allows the total conversion of D,L-5-monosubstituted hydantoins into optically pure D- or L-amino acids. -!- The enzyme from Alcaligenes xylosoxidans has broad specificity for carbamoyl-L-amino acids, although it is inactive on the carbamoyl derivatives of glutamate, aspartate, arginine, tyrosine or tryptophan. -!- The enzyme from Sinorhizobium meliloti requires a divalent cation for activity and can hydrolyze N-carbamoyl-L-tryptophan as well as N-carbamoyl L-amino acids with aliphatic substituents. -!- The enzyme is inactive on derivatives of D-amino acids. -!- In addition to N-carbamoyl L-amino acids, the enzyme can also hydrolyze formyl and acetyl derivatives to varying degrees.
|
UniProtKB Entries (1)
| Q53389 |
AMAB2_GEOSE
Geobacillus stearothermophilus
N-carbamoyl-L-amino acid hydrolase
|
PDB Structure
| PDB | 3N5F |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Mutational and structural analysis of L-N-carbamoylase reveals new insights into a peptidase m20/m25/m40 family member.
J.Bacteriol.
|
