CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.60 | 4-Layer Sandwich |
|
3.60.110 | Nitrilase/N-carbamoyl-D-aminoacid amidohydrolase |
|
3.60.110.10 | Carbon-nitrogen hydrolase |
Domain Context
CATH Clusters
| Superfamily | Carbon-nitrogen hydrolase |
| Functional Family |
Enzyme Information
| 3.5.1.77 |
N-carbamoyl-D-amino-acid hydrolase.
based on mapping to UniProt Q44185
N-carbamoyl-D-amino acid + H(2)O = D-amino acid + NH(3) + CO(2).
-!- This enzyme, along with EC 3.5.1.87, 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. -!- Has strict stereospecificity for N-carbamoyl-D-amino acids and does not act upon the corresponding L-amino acids or N-formyl amino acids, N-carbamoyl-sarcosine, -citrulline, -allantoin and -ureidopropanoate, which are substrates for other amidohydrolases.
|
UniProtKB Entries (1)
| Q44185 |
DCAS_RHIRD
Agrobacterium tumefaciens
N-carbamoyl-D-amino acid hydrolase
|
PDB Structure
| PDB | 1FO6 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure and site-directed mutagenesis studies of N-carbamoyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter reveals a homotetramer and insight into a catalytic cleft.
J.Mol.Biol.
|
