CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.200 | Peptidase S8/S53 domain |
Domain Context
CATH Clusters
| Superfamily | Peptidase S8/S53 domain |
| Functional Family | Proteinase K |
Enzyme Information
| 3.4.21.111 |
Aqualysin 1.
based on mapping to UniProt P08594
Exhibits low specificity toward esters of amino acids with small hydrophobic or aromatic residues at the P1 position.
-!- This enzyme from the extreme thermophile, Thermus aquaticus, is an alkaline serine peptidase. -!- It has three subsites, S1, S2, and S3, in the substrate binding site. -!- The preferred amino acids at the S1 site are Ala and Phe, at the S2 site are Ala and norleucine and at the S3 site are Phe and Ile. -!- These specificities are similar to those of EC 3.4.21.62 and EC 3.4.21.64. -!- The enzyme displays broad specificity for cleavage of insulin B-chain and hydrolyzes elastin substrates such as succinyl-(Ala)(n)-p- nitroanilide (n = 1,2,3) and some peptide esters. -!- Belongs to peptidase family S8A.
|
UniProtKB Entries (1)
| P08594 |
AQL1_THEAQ
Thermus aquaticus
Aqualysin-1
|
PDB Structure
| PDB | 4DZT |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Aqualysin I: the crystal structure of a serine protease from an extreme thermophile, Thermus aquaticus YT-1
To be Published
|