CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.150 | DNA polymerase; domain 1 |
|
1.10.150.900 |
Domain Context
CATH Clusters
| Superfamily | 1.10.150.900 |
| Functional Family | Aminoacylase-1, putative |
Enzyme Information
| 3.5.1.14 |
N-acyl-aliphatic-L-amino acid amidohydrolase.
based on mapping to UniProt Q03154
(1) An N-acyl-aliphatic-L-amino acid + H(2)O = an aliphatic L-amino acid + a carboxylate. (2) An N-acetyl-L-cysteine-S-conjugate + H(2)O = an L-cysteine-S- conjugate + acetate.
-!- The enzyme is found in animals and is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate). -!- It acts on mercapturic acids (S-conjugates of N-acetyl-L-cysteine) and neutral aliphatic N-acyl-alpha-amino acids. -!- Some bacterial aminoacylases demonstrate substrate specificity of both EC 3.5.1.14 and EC 3.5.1.114. -!- Cf. EC 3.5.1.15 and EC 3.5.1.114.
|
UniProtKB Entries (1)
| Q03154 |
ACY1_HUMAN
Homo sapiens
Aminoacylase-1
|
PDB Structure
| PDB | 1Q7L |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Spodoptera |
| Primary Citation |
Essential roles of zinc ligation and enzyme dimerization for catalysis in the aminoacylase-1/M20 family.
J.Biol.Chem.
|
