EC Number |
Activating Compound |
Reference |
---|
3.4.24.19 | Enhancer glycoprotein |
bound to the carboxyl propeptide of type I procollagen |
31034 |
3.4.24.19 | Enhancer glycoprotein |
characterization |
31043 |
3.4.24.19 | Enhancer glycoprotein |
enhancer may play a regulatory role in procollagen processing |
31043 |
3.4.24.19 | Enhancer glycoprotein |
enhances activity of C-proteinase |
31034, 31036 |
3.4.24.19 | Enhancer glycoprotein |
stimulates activity |
668838 |
3.4.24.19 | Frizzled-related protein |
secreted Frizzled-related protein sFRP2 serves as a direct enhancer of procollagen C proteinase activity of tolloid-like metalloproteinases. The level of fibrosis, in which procollagen processing by tolloid-like proteinases has a rate-limiting role, is markedly reduced in Sfrp2-null mice subjected to myocardial infarction. This reduced level of fibrosis is accompanied by significantly improved cardiac function |
700348 |
3.4.24.19 | heparin |
stimulation of BMP-1 activity by procollagen C-proteinase enhancer-1 is further increased by the presence of 0.05 mg/ml heparin |
712425 |
3.4.24.19 | heparin sulfate |
in the presence of both procollagen C-proteinase enhancer-1 and heparin or heparan sulfate, the activity of BMP-1 is further stimulated |
712425 |
3.4.24.19 | more |
both PCPE1 and PCPE2 are located in the extracellular matrix, where they facilitate bone morphogenetic protein 1 (BMP1) cleavage of C-terminal procollagen propeptides. PCPE2 and PCPE1 have different tissue distributions and heparin-binding affinities, suggesting a functional divergence. PCPE2 is heavily expressed in heart tissue in contrast to PCPE1. Both PCPE1 and PCPE2 have two CUB (Complement C1r/C1s, Uegf, Bmp1) domains separated by a short linker region, with each domain consisting of about 110 residues containing a beta-sandwich fold that mediates a variety of protein-protein interactions. Phenotype of PCPE2-/- mice, overview |
754110 |
3.4.24.19 | PCPE-1 |
enhances degredation of procollagen type I 5 fold, enhances C-terminal processing of procollagen type III when this substrate is in its native, disulfide-bonded conformation, has no effect on the in vitro BMP-1 processing of procollagen VII, procollagen V N-propeptide, laminin 5 gamma2 chain, osteoglycin, prolysyl oxidase or chordin |
669352 |