3.4.17.15	glycoprotein	recombinant enzyme expressed in Pichia pastoris	
3.4.17.15	proteolytic modification	synthesized as procarboxypeptidase A2	
3.4.17.15	proteolytic modification	the proCPA2 is activated by cleavage by trypsin	
3.4.17.15	proteolytic modification	the proCPA2 is activated by proteoltyic cleavage	
3.4.17.15	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