Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | the triad for binding of the activation peptide consists of Asp, Phe, and Trp residues | Paralichthys olivaceus |
Cloned (Comment) | Organism |
---|---|
DNA and amino acid sequence determination and analysis of the preproenzyme, phylogenetic analysis | Paralichthys olivaceus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | zinc-metallopeptidase, binding residues are H69, E72, and H196 | Paralichthys olivaceus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Paralichthys olivaceus | Q8AXN5 | preprocarboxypeptidase A2; Japanese flounder, female | - |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | the proCPA2 is activated by proteoltyic cleavage | Paralichthys olivaceus |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
Similar to that of carboxypeptidase A (EC 3.4.17.1), but with a preference for bulkier C-terminal residues | residues Glu270 and Arg127 are important for activity, the catalytic triad consists of Ile275, Tyr248, and Ala250, residues at positions 202, 254, and 268 are important for substrate specificity | Paralichthys olivaceus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
intestine | - |
Paralichthys olivaceus | - |
pancreas | - |
Paralichthys olivaceus | - |
Synonyms | Comment | Organism |
---|---|---|
CPA2 | - |
Paralichthys olivaceus |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Paralichthys olivaceus | sequence calculation | - |
8.7 |