3.4.17.15: carboxypeptidase A2
This is an abbreviated version!
For detailed information about carboxypeptidase A2, go to the full flat file.
Reaction
Similar to that of carboxypeptidase A (EC 3.4.17.1), but with a preference for bulkier C-terminal residues =
Synonyms
ADA2, carboxypeptidase-A2, CP-A2, CPA2
ECTree
Advanced search results
Posttranslational Modification
Posttranslational Modification on EC 3.4.17.15 - carboxypeptidase A2
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
proteolytic modification
proteolytic modification
-
the proCPA2 is activated by cleavage by trypsin
proteolytic modification
in silico conversion of zymogen into the primary cleavage state using available X-ray structures to investigate its spontaneous dissociation process of the prosegment from its associated enzyme domain using steered molecular dynamics simulation. The cleavage substantially destabilizes most of the hydrogen bonds at the prosegment-enzyme interface. During prosegment unbinding, the enzyme shows first rupture in the globular domain and then in the connecting segment
proteolytic modification
the proCPA2 is activated by proteoltyic cleavage