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3.4.24.19: procollagen C-endopeptidase

This is an abbreviated version!
For detailed information about procollagen C-endopeptidase, go to the full flat file.

Word Map on EC 3.4.24.19

Reaction

cleavage of the C-terminal propeptide at Ala-/-Asp in type I and II procollagens and at Arg-/-Asp in type III =

Synonyms

BMP-1, BMP1, bone morphogenetic protein 1, bone morphogenetic protein 1/tolloid, bone morphogenetic protein-1, bone morphogenic protein 1, Carboxy-terminal endopeptidase, carboxy-terminal procollagen peptidase, Carboxyl procollagen peptidase, carboxyl-procollagen peptidase, Carboxyprocollagen peptidase, dorsal-ventral patterning protein tolloid, mammalian tolloid, Mammalian tolloid protein, More, mTId, MtlD, PCP, PCP-1, PCP-2, Peptidase, procollagen C-terminal, procollagen C-peptidase, Procollagen C-proteinase, Procollagen C-terminal proteinase, Procollagen carboxy-terminal proteinase, Procollagen carboxypeptidase, Procollagen peptidase, Proteinase, procollagen C-terminal, suBMP-1, TId, Tld, tolloid, Type I procollagen C-proteinase, XBMP1-A, XBMP1-B

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.19 procollagen C-endopeptidase

Activating Compound

Activating Compound on EC 3.4.24.19 - procollagen C-endopeptidase

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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Enhancer glycoprotein
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Frizzled-related protein
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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
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heparin
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stimulation of BMP-1 activity by procollagen C-proteinase enhancer-1 is further increased by the presence of 0.05 mg/ml heparin
heparin sulfate
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in the presence of both procollagen C-proteinase enhancer-1 and heparin or heparan sulfate, the activity of BMP-1 is further stimulated
PCPE-1
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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
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procollagen C-endopeptidase enhancer protein 1
PCPE1, a glycoprotein located in the extracellular matrix, enhances the cleavage of C-terminal procollagen by bone morphogenetic protein 1 (BMP1)
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procollagen C-endopeptidase enhancer protein 2
PCPE2, a 52-kDa glycoprotein located in the extracellular matrix, enhances the cleavage of C-terminal procollagen by bone morphogenetic protein 1 (BMP1). PCPE2 is not essential for in vivo pro-apoA-I processing. PCPE2 confers atheroprotection to apoA-I by enhancing BMP1-mediated catalytic cleavage, converting pro-apoA-I to mature apoA-I, and stimulating ABCA1-mediated cholesterol flux, but pro-apoA-I processing is not altered in the case of PCPE2 deficiency
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procollagen C-proteinase enhancer 1
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procollagen C-proteinase enhancer 2
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specifically activates bone morphogenetic protein-1, the CUB domains CUB1 and CUB2 of procollagen C-proteinase enhancer 1 are capable of enhancing BMP-1 activity and binding to a mini-procollagen substrate with nanomolar affinity
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procollagen C-proteinase enhancer-1
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procollagen C-proteinase enhancer-2
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procollagen C-proteinase enhancer-2 (PCPE2) interacts with BMP-1 and pro-apoAI to form a ternary pro-apoAI/BMP-1/PCPE2 complex, PCPE2 enhances the BMP-1 cleavage and maturation of pro-apoAI
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TGFbeta
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increases the expression of BMP-1 and Tld in human dermal fibroblasts
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additional information
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
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