EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.24.B7 | glycoprotein |
2 N-glycosylation sites at residues 64 and 133 |
650768 |
| 3.4.24.B7 | glycoprotein |
two (N64, N221) of the three possible N-glycosylation sites in MMP-26 are N-glycosylated, and N-glycosylation is not required for ER localization |
755387 |
| 3.4.24.B7 | more |
MMP-26 is only active after treatement with reducing agents |
708392 |
| 3.4.24.B7 | more |
no activation of the proform by organomercurial treatment |
652254 |
| 3.4.24.B7 | proteolytic modification |
autoactivation by autocleavage of the proform at sequence Lys-Lys-Gln59-Gln60-Phe-His, His81 plays a significant role in functional modification |
652254 |
| 3.4.24.B7 | proteolytic modification |
autocatalytically activated in cells and tissues |
668149 |
| 3.4.24.B7 | proteolytic modification |
MMP-26 autoactivates |
707115 |
| 3.4.24.B7 | proteolytic modification |
propeptides sequence PHCGVPDGSD |
652014 |
| 3.4.24.B7 | proteolytic modification |
two of the major autolytic sites are Leu49/-Thr50 and Ala75/-Leu76, which still left the cysteine switch sequence intact |
652303 |
