EC Number | Cloned (Comment) | Organism |
---|---|---|
3.4.14.5 | expression in Escherichia coli | Lactococcus lactis |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.4.14.5 | purified recombinant enzyme, hanging drop method using 5-10% PEG 4000, pH 5.2, 18°C, preparation of heavy atom derivatives, X-ray diffraction structure determination and analysis at 2.2 A resolution | Lactococcus lactis |
3.4.14.11 | hanging drop method | Lactococcus lactis |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.4.14.11 | membrane | the C-terminal moiety probably plays a role in tropism of the enzyme towards the cellular membrane | Lactococcus lactis | 16020 | - |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.14.5 | Lactococcus lactis | P22346 | ssp. cremoris | - |
3.4.14.5 | Lactococcus lactis | Q9CE11 | ssp. cremoris | - |
3.4.14.11 | Lactococcus lactis | P22346 | - |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
3.4.14.5 | release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline | active site structure and accessibility | Lactococcus lactis |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.4.14.5 | dimer | homodimeric enzyme, crystal structure, overall fold and structure of the dimer and dimer interface, overview | Lactococcus lactis |
3.4.14.11 | 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 |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.4.14.5 | More | enzyme belongs to the SC clan that includes 38 families of peptidases, and is the prototype of the S15 family | Lactococcus lactis |
3.4.14.5 | PepX | - |
Lactococcus lactis |
3.4.14.5 | X-PDAP | - |
Lactococcus lactis |
3.4.14.5 | X-prolyl dipeptidyl aminopeptidase | - |
Lactococcus lactis |