ENZYME entry: EC 3.4.21.111
Accepted Name |
Aqualysin 1.
|
Alternative Name(s) |
Caldolysin. |
Reaction catalysed |
Exhibits low specificity toward esters of amino acids with small hydrophobic or aromatic residues at the P1 position |
Comment(s) |
- 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.
|
Cross-references |
PROSITE | PDOC00125 |
BRENDA | 3.4.21.111 |
EC2PDB | 3.4.21.111 |
ExplorEnz | 3.4.21.111 |
PRIAM enzyme-specific profiles | 3.4.21.111 |
KEGG Ligand Database for Enzyme Nomenclature | 3.4.21.111 |
IUBMB Enzyme Nomenclature | 3.4.21.111 |
IntEnz | 3.4.21.111 |
MEDLINE | Find literature relating to 3.4.21.111 |
MetaCyc | 3.4.21.111 |
UniProtKB/Swiss-Prot |
|
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