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Information on EC 3.4.24.19 - procollagen C-endopeptidase and Organism(s) Mus musculus and UniProt Accession P98063

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.19 procollagen C-endopeptidase
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This record set is specific for:
Mus musculus
UNIPROT: P98063 not found.
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The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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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, tolloid, procollagen c-proteinase, pcp-2, pcp-1, bone morphogenetic protein 1, bone morphogenetic protein-1, mammalian tolloid, procollagen c-endopeptidase, procollagen peptidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
bone morphogenetic protein 1
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BMP-1
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bone morphogenetic protein 1
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Carboxy-terminal endopeptidase
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-
-
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carboxy-terminal procollagen peptidase
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Carboxyl procollagen peptidase
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-
-
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carboxyl-procollagen peptidase
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Carboxyprocollagen peptidase
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-
-
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mammalian tolloid
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Mammalian tolloid protein
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-
-
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PCP-1
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PCP-2
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Peptidase, procollagen C-terminal
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-
-
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procollagen C-peptidase
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Procollagen C-proteinase
Procollagen C-terminal proteinase
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-
-
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Procollagen carboxy-terminal proteinase
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-
-
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Procollagen carboxypeptidase
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-
-
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Procollagen peptidase
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-
-
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Proteinase, procollagen C-terminal
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-
-
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Type I procollagen C-proteinase
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-
-
-
additional information
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Bone morphogenetic protein-1 is identical with procollagen C-proteinase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
68651-95-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
pro-apoA-I + H2O
apoA-I + apoA-I propeptide
show the reaction diagram
-
-
-
?
procollagen + H2O
collagen + collagen propeptide
show the reaction diagram
-
-
-
?
procollagen I + H2O
pCcollagen + oligopeptide
show the reaction diagram
-
-
-
-
?
Procollagen type I + H2O
Type I pNcollagen + C-propeptides
show the reaction diagram
Procollagen type II + H2O
Type II pNcollagen + C-propeptides
show the reaction diagram
Procollagen type III + H2O
Type III pNcollagen + C-propeptides
show the reaction diagram
Type I/III/III pCcollagen + H2O
Type I/II/III collagen + C-propeptides
show the reaction diagram
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pCcollagen is an intermediate in the processing of procollagen to collagen containing the carboxyl propeptides but not the amino propeptides
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
pro-apoA-I + H2O
apoA-I + apoA-I propeptide
show the reaction diagram
-
-
-
?
procollagen + H2O
collagen + collagen propeptide
show the reaction diagram
-
-
-
?
procollagen I + H2O
pCcollagen + oligopeptide
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
zinc metalloproteinase
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
a common inhibitor of several astacin metalloproteases
1,10-phenanthroline
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6-aminohexanoic acid
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Amines
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Blood serum
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-
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decanoyl-Arg-Val-Lys-Arg-chloromethylketone
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diisopropylphosphofluoridate
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weak
EDTA
-
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EGTA
-
-
L-arginine
-
-
L-lysine
-
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leupeptin
-
not
metal chelators
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-
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pepstatin
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not
additional information
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not: inhibitors of serine
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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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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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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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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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of cultured mouse fibroblasts
Manually annotated by BRENDA team
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throughout the mesenchyme of developing embryonic tissue
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
additional information
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in developing membranous and endochondral bones, in sections of murine hind limp and femoral growth plate
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
postnatal rat tail and postnatal mouse tail tendon, C-proteinase activity is detected in trans-Golgi network and pre-trans-Golgi network compartments
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme encoded by bmp1 belongs to the BTP cluster of the astacin enzyme family. Structure-activity relationship of astacin metalloproteases, EDTA is used to dock into the active site cleft of the astacins to know the interaction network and to identify the important residues for binding, comparative three-dimensional structure homology modeling and docking study, and potential binding site, detailed overview
physiological function
BMP1, in addition to catalyzing procollagen processing, removes the apoA-I six-amino acid propeptide. BMP1-PCPE2 processing of the apoA-I propeptide might stimulate nHDL assembly. PCPE2 enhances the BMP1-mediated cleavage of propeptides from procollagen. 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
metabolism
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the N-propeptides are removed first, most probably in the Golgi or in the ERGIC (ER-Golgi intermediate compartment). In contrast, the C-propeptides are cleaved in a post-Golgi compartment
additional information
the hydrogen bonding residue of the enzyme is Glu219, comparative three-dimensional structure homology modeling (template crystal structure PDB ID 3EDH) and docking study, and potential binding site, detailed overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BMP1_MOUSE
991
0
111666
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
111600
-
mTld
125000
-
mouse, gel filtration
80000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 80000, mouse, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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homozygous null mice lacking PCBs encoded by BMP-1 are perinatally lethal and have reduced ossification of skull bones and defects in formation of the ventral body wall, procollagen processing and collagen fibrillogenesis
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene mbmp1, sequence comparisons
recombinant bone morphogenetic protein-1 produced by a baculovirus system
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kessler, E.; Adar, R.
Type I procollagen C-proteinase from mouse fibroblasts. Purification and demonstration of a 55-kDa enhancer glycoprotein
Eur. J. Biochem.
186
115-121
1989
Mus musculus
Manually annotated by BRENDA team
Kadler, K.E.; Watson, R.B.
Procollagen C-peptidase: procollagen C-proteinase
Methods Enzymol.
248
771-781
1995
Gallus gallus, Mus musculus
Manually annotated by BRENDA team
Kessler, E.; Takahara, K.; Biniaminov, L.; Brusel, M.; Greenspan, D.S.
Bone morphogenic protein-1: the type I procollagen C-proteinase
Science
271
360-362
1971
Mus musculus
Manually annotated by BRENDA team
Kessler, E.; Adar, R.; Goldberg, B.; Niece, R.
Partial purification and characterization of a procollagen C-proteinase from the culture medium of mouse fibroblasts
Coll. Relat. Res.
6
249-266
1986
Mus musculus
Manually annotated by BRENDA team
Adar, R.; Kessler, E.; Goldberg, B.
Evidence for a protein that enhances the activity of type I procollagen C-proteinase
Coll. Relat. Res.
6
267-277
1986
Mus musculus
Manually annotated by BRENDA team
Kessler, E.
Procollagen C-endopeptidase
Handbook of Proteolytic Enzymes(Barrett,A. J. ,Rawlings,N. D. ,Woessner,J. F. ,Eds. )Academic Press
1
609-617
2004
Gallus gallus, Homo sapiens, Mus musculus, Rattus norvegicus, Strongylocentrotus purpuratus, Xenopus laevis
-
Manually annotated by BRENDA team
Kobayashi, K.; Luo, M.; Zhang, Y.; Wilkes, D.C.; Ge, G.; Grieskamp, T.; Yamada, C.; Liu, T.C.; Huang, G.; Basson, C.T.; Kispert, A.; Greenspan, D.S.; Sato, T.N.
Secreted Frizzled-related protein 2 is a procollagen C proteinase enhancer with a role in fibrosis associated with myocardial infarction
Nat. Cell Biol.
11
46-55
2009
Mus musculus
Manually annotated by BRENDA team
Canty-Laird, E.G.; Lu, Y.; Kadler, K.E.
Stepwise proteolytic activation of type I procollagen to collagen within the secretory pathway of tendon fibroblasts in situ
Biochem. J.
441
707-717
2012
Gallus gallus, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Chaudhuri, A.; Chakraborty, S.
Structure-activity relationship of astacin metalloproteases A comparative study using EDTA
Curr. Enzyme Inhib.
14
131-140
2018
Drosophila melanogaster (P25723), Mus musculus (P98063), Xenopus laevis (P98070)
-
Manually annotated by BRENDA team
Pollard, R.D.; Blesso, C.N.; Zabalawi, M.; Fulp, B.; Gerelus, M.; Zhu, X.; Lyons, E.W.; Nuradin, N.; Francone, O.L.; Li, X.A.; Sahoo, D.; Thomas, M.J.; Sorci-Thomas, M.G.
Procollagen C-endopeptidase enhancer protein 2 (PCPE2) reduces atherosclerosis in mice by enhancing scavenger receptor class B1 (SR-BI)-mediated high-density lipoprotein (HDL)-cholesteryl ester uptake
J. Biol. Chem.
290
15496-15511
2015
Mus musculus (P98063)
Manually annotated by BRENDA team