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 P77425
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.
|
| 3.5.3.9 |
Allantoate deiminase.
based on mapping to UniProt P77425
Allantoate + H(2)O = (S)-ureidoglycine + NH(3) + CO(2).
-!- This enzyme is part of the ureide pathway, which permits certain organisms to recycle the nitrogen in purine compounds. -!- This enzyme, which liberates ammonia from allantoate, is present in plants and bacteria. -!- In plants it is localized in the endoplasmic reticulum. -!- Requires manganese.
|
| 3.5.3.- |
In linear amidines.
based on mapping to UniProt P77425
|
| 3.5.3.4 |
Allantoicase.
based on mapping to UniProt P77425
Allantoate + H(2)O = (S)-ureidoglycolate + urea.
-!- Also hydrolyzes (R)-ureidoglycolate to glyoxylate and urea.
|
UniProtKB Entries (1)
| P77425 |
ALLC_ECOLI
Escherichia coli K-12
Allantoate amidohydrolase
|
PDB Structure
| PDB | 1Z2L |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structural analysis of a ternary complex of allantoate amidohydrolase from Escherichia coli reveals its mechanics.
J.Mol.Biol.
|