EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.23.39 | proteolytic modification |
plasmepsin II is produced as a precursor. The propart region, about 120 residues, is more than twice as long as those of archetypal zymogens |
648190 |
| 3.4.23.39 | proteolytic modification |
pro-plasmepsin II is transported through the secretory system to cytostomal vacuoles and then is carried along with its substrate hemoglobin to the food vacuole where it is proteolytically processed to mature PMII |
669571 |
| 3.4.23.39 | proteolytic modification |
proplasmepsin maturation appears to require acidic conditions, proplasmepsin maturation may not be autocatalytic in vivo |
648184 |
| 3.4.23.39 | proteolytic modification |
protein is expressed as an inactive zymogen with a large prosegment |
710468 |
| 3.4.23.39 | proteolytic modification |
PSM2 is less active after maturation. At pH 2.2 PSM2 activity is observed only without maturation |
708888 |
| 3.4.23.39 | proteolytic modification |
recombinant proplasmepsin II autoactivates at acidic pH, but the location of the cleavage site varies dependening on the conditions used |
648185 |
| 3.4.23.39 | proteolytic modification |
the large N-terminal displacement and the interdomain shift from the proenzyme structure to active plasmepsin are promoted by essential dynamics sampling. An intermediate, stabilized by electrostatic interactions between the catalytic dyad and the N-terminus of mature plasmepsin, is observed along all activation trajectories. The stabilizing interactions in the activation intermediate of plasmepsin are similar to those in the X-ray structure of pepsinogen. The catalytic aspartates act as hydrogen bond acceptors for the N-terminal amino group and the Ser2 hydroxyl in plasmepsin, and the side chains of Lys36pro and Tyr9 in pepsinogen |
701129 |
| 3.4.23.39 | proteolytic modification |
the PMII zymogen utilizes a prosegment-catalyzed folding mechanism |
717158 |
| 3.4.23.39 | proteolytic modification |
the processing of PM II and IV occurs via an intra- and inter-molecular autocatalytic event as well as via a transcatalytic event between them |
669157 |
| 3.4.23.39 | proteolytic modification |
the proenzyme has an unusually long propart of 125 amino acid residues that mediates type II membrane anchoring of the proenzyme, activation occurs by removal of the propart, proplasmepsin II can autoactivate at acidic pH |
648182 |
