EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.24.63 | glycoprotein |
- |
-, 31024, 683206, 735161 |
| 3.4.24.63 | glycoprotein |
deglycosylation of recombinant enzyme by peptide-N-glycosidase |
733822 |
| 3.4.24.63 | glycoprotein |
deglycosylation of recombinant meprin beta by PNGaseF |
752709 |
| 3.4.24.63 | glycoprotein |
N-glycosidase F-sensitive |
31380 |
| 3.4.24.63 | glycoprotein |
the enzyme is highly glycosylated |
-, 733947 |
| 3.4.24.63 | glycoprotein |
the recombinant enzyme expressed in Pichia pastoris is N-glycosylated. Deglycosylation by endoglycosidase H does not alter the kinetics of the enzyme significantly |
755294 |
| 3.4.24.63 | proteolytic modification |
activation of meprin beta by proteolytic cleavage. Meprin beta contains a conserved sequence motif, which gives rise to enzymatic activation by tryptic serine proteases. Pancreatic trypsin performs this activation in the gut. Meprin beta cannot be activated by plasmin in the gut. In skin, the human tissue kallikrein-related peptidase 4 (KLK4), KLK5, and KLK8, cleave off the propeptide of meprin beta |
754592 |
| 3.4.24.63 | proteolytic modification |
activation of recombinant zymogen enzyme by trypsin |
734296 |
| 3.4.24.63 | proteolytic modification |
activation of the inactive zymogen by proteases |
733288 |
| 3.4.24.63 | proteolytic modification |
matriptase-2 (MT-2), a type 2 transmembrane protein, fully activates meprin beta at the cell surface |
753697 |
