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Literature summary for 3.4.14.11 extracted from
- The structural basis for catalysis and specificity of the X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis (2002), Structure, 10, 1383-1394.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| hanging drop method | Lactococcus lactis |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | the C-terminal moiety probably plays a role in tropism of the enzyme towards the cellular membrane | Lactococcus lactis | 16020 | - |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Lactococcus lactis | P22346 | - |
- |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | each monomer is composed of four domains. The larger one presents an alpha/beta hydrolase fold and comprises the active site serine. The specificity pocket is mainly built by residues from a small helical domain which is, together with the N-terminal domain, essential for dimerization | Lactococcus lactis |
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