EC Number   |
Posttranslational Modification |
Reference |
|---|
   1.4.3.13 | glycoprotein |
- |
391741, 391742, 698383 |
| 1.4.3.13 | glycoprotein |
2 NRT-consensus sequences for N-glycosylation |
659558 |
| 1.4.3.13 | glycoprotein |
N-glycans at Asn-455 and Asn-644 are essential for proper folding and secretion of the enzyme. The N-glycan at Asn-644 enhances the solubility and stability of the enzyme catalytic domain |
725545 |
| 1.4.3.13 | glycoprotein |
N-glycosylated as 50 kDa preproprotein |
391742 |
| 1.4.3.13 | glycoprotein |
the LOX propeptide is glycosylated. Glycosylation is not required for secretion and extracellular processing of pro-enzyme but it is required for optimal enzyme activity of the resulting mature enzyme |
725597 |
| 1.4.3.13 | more |
LOX suffers different posttranslational modifications including signal peptide cleavage, glycosylation, copper incorporation and formation of the lysyl-tyrosyl-quinone cofactor |
686904 |
| 1.4.3.13 | proteolytic modification |
activation of the proenzyme by cleavage, enzyme contains a BMP-1 cleavage site |
658190 |
| 1.4.3.13 | proteolytic modification |
enzyme contains a catalysis-suppressing propeptide signal domain at the N-terminus |
659558 |
| 1.4.3.13 | proteolytic modification |
LOX is secreted as a glycosylated proenzyme with a MW of 50 kDa, and is proteolytically processed by procollagen C proteinase, i.e. bone morphogenic protein-1, into a mature, biologically active MW 32 kDa form |
698383 |
| 1.4.3.13 | proteolytic modification |
LOX, LOXL1, LOXL2, LOXL3, and LOXL4, enzymes contain a conserved BMP-1 cleavage site at Gly134-Asp135 and Ser337-Asp338 |
660423 |
