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EC Number
Posttranslational Modification
Commentary
Reference
3.4.17.15
proteolytic modification
synthesized as procarboxypeptidase A2
647257
3.4.17.15
proteolytic modification
the proCPA2 is activated by cleavage by trypsin
667298
,
669188
3.4.17.15
glycoprotein
recombinant enzyme expressed in Pichia pastoris
669188
3.4.17.15
proteolytic modification
the proCPA2 is activated by proteoltyic cleavage
668310
,
670816
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
732350
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