A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.
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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UniProtKB/Swiss-Prot entries corresponding to 3.4.21.-
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