3.4.24.3: microbial collagenase
This is an abbreviated version!
For detailed information about microbial collagenase, go to the full flat file.
Word Map on EC 3.4.24.3
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3.4.24.3
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peyronie
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contracture
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collagenases
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hemorrhage
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cartilage
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penile
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curvature
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intracerebral
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intralesional
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tendon
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pepsin
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basement
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procollagens
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hydroxyproline
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metacarpophalangeal
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noncollagenous
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interphalangeal
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fasciectomy
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gelatinase
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hematoma
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erectile
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palpable
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collagenase-induced
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collagen-like
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satisfaction
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dentin
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flexion
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intrastriatal
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albuginea
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traction
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debridement
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palmar
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triple-helical
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ointment
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demineralized
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nonsurgical
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collagen-binding
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3hproline
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bruising
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stromelysin
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hydroxylysine
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bother
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collagenase-treated
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microfibrillar
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ich-induced
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dispase
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plication
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pepsin-resistant
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perihematomal
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collagenase-digestible
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pharmacology
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medicine
- 3.4.24.3
- peyronie
- contracture
- collagenases
- hemorrhage
- cartilage
-
penile
-
curvature
-
intracerebral
-
intralesional
- tendon
- pepsin
-
basement
- procollagens
- hydroxyproline
-
metacarpophalangeal
-
noncollagenous
-
interphalangeal
-
fasciectomy
- gelatinase
-
hematoma
-
erectile
-
palpable
-
collagenase-induced
-
collagen-like
-
satisfaction
- dentin
-
flexion
-
intrastriatal
-
albuginea
-
traction
-
debridement
-
palmar
-
triple-helical
-
ointment
-
demineralized
-
nonsurgical
-
collagen-binding
-
3hproline
-
bruising
- stromelysin
- hydroxylysine
-
bother
-
collagenase-treated
-
microfibrillar
-
ich-induced
-
dispase
-
plication
-
pepsin-resistant
-
perihematomal
-
collagenase-digestible
- pharmacology
- medicine
Reaction
Digestion of native collagen in the triple helical region at -/-Gly bonds. With synthetic peptides, a preference is shown for Gly at P3 and P1', Pro and Ala at P2 and P2', and hydroxyproline, Ala or Arg at P3' =
Synonyms
120 kDa collagenase, Achromobacter iophagus collagenase, aspergillopeptidase C, azocollase, bacterial collagenase, bacterial collagenase V, BC_2466, CCA, ChC, class I collagenase, class II collagenase, class III collagenase, clostridial collagenase, clostridial collagenase A, clostridiopeptidase A, clostridiopeptidase I, clostridiopeptidase II, Clostridium histolyticum class II collagenase, Clostridium histolyticum collagenase, ColA, ColG, ColH, collagen peptidase, collagen protease, collagenase, collagenase A, collagenase clostridium histolyticum, collagenase G, collagenase H, collagenase I, collagenase MMP-1, collagenase T, ColT, Dupuytren clostridium histolyticum, Dupuytren collagenase, EC 3.4.24.8, EC 3.4.4.19, EC 3.4.99.5, kollaza, M9-peptidase, matirx metalloproteinase-18, matrix metalloproteinase-1, metallocollagenase, metalloproteinase ColB, metalloproteinase-1, microbial collagenase, MMP-1, More, nucleolysin, peptidase, clostridio-, A, proteinase, Clostridium histolyticum, A, soycollagestin, thermophilic collagenolytic protease, type I collagenase, type II collagenase, VMC peptidase
ECTree
3.4.24.3 microbial collagenaseAdvanced search results
results (
results (Engineering
Engineering on EC 3.4.24.3 - microbial collagenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D904A
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mutant enzyme with increased MW in presence of Ca2+ and decreased MW in presence of 1 mM EGTA, determined by gel filtration
D927A
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mutant enzyme with increased MW in presence of Ca2+ and slightly decreased MW in presence of 1 mM EGTA, determined by gel filtration
D930A
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mutant enzyme with increased MW in presence of Ca2+ and slightly decreased MW in presence of 1 mM EGTA, determined by gel filtration
E414Q
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mutant enzyme with a with a lower level of hydrolytic activity against insoluble collagen compared to wild-type enzyme
E899A
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mutant enzyme with increased MW in presence of Ca2+ and decreased MW in presence of 1 mM EGTA, determined by gel filtration
E901A
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mutant enzyme with increased MW in presence of Ca2+ and decreased MW in presence of 1 mM EGTA, determined by gel filtration
N903A
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mutant enzyme with increased MW in presence of Ca2+ and slightly increased MW in presence of 1 mM EGTA, determined by gel filtration
S906F
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mutant enzyme with slightly decreased MW in presence of Ca2+ ad slightly increased MW in presence of 1 mM EGTA, determined by gel filtration
additional information
additional information
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addition of an N-terminal His-tag. The Michaelis-Menten constant of ColT increases by approximately 60%. Expression of a truncated construct Y53-A506 which stops shortly after the third zinc binding residue and consitstent with the prediction of a minimal catalytic domain. The construct shows no catalytic activity at all, despite containing all zinc binding residues including the catalytic glutamate that is supposed to act as general base
additional information
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addition of an N-terminal His-tag. The Michaelis-Menten constant of ColG and ColH increases by approximately 50% and 60%, respectively
additional information
an activator-deletion construct, containing only the segment Lys396-Lys1118, shows 100% activity against small peptidic substrates as compared to the full-length ColG protease. The peptidase domain alone is completely inactive toward collagen substrates. Full collagenolytic activity is, however, contained in the segment Tyr119-Gly790, comprising the activator and peptidase domains
additional information
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an activator-deletion construct, containing only the segment Lys396-Lys1118, shows 100% activity against small peptidic substrates as compared to the full-length ColG protease. The peptidase domain alone is completely inactive toward collagen substrates. Full collagenolytic activity is, however, contained in the segment Tyr119-Gly790, comprising the activator and peptidase domains
additional information
construction of fusion proteins between the collagen-binding domain (CBD) and polycystic kidney disease (PKD) domain of Clostridium histolyticum class II collagenase and basic fibroblast growth factor. Both fusion proteins bFGF-CBD and bFGF-PKD-CBD promote the in vitro proliferation of periosteal mesenchymal cells. Both bFGF-CBD and bFGF-PKD-CBD induce periosteal bone formation at higher rates than collagen sheet alone and bFGF. bFGF-PKD-CBD markedly enhances bone formation and has higher collagen-binding ability than bFGF-CBD in in vitro protein release assays
additional information
-
construction of fusion proteins between the collagen-binding domain (CBD) and polycystic kidney disease (PKD) domain of Clostridium histolyticum class II collagenase and basic fibroblast growth factor. Both fusion proteins bFGF-CBD and bFGF-PKD-CBD promote the in vitro proliferation of periosteal mesenchymal cells. Both bFGF-CBD and bFGF-PKD-CBD induce periosteal bone formation at higher rates than collagen sheet alone and bFGF. bFGF-PKD-CBD markedly enhances bone formation and has higher collagen-binding ability than bFGF-CBD in in vitro protein release assays
additional information
an activator deletion construct of ColG (Lys396-Lys1118) is fully active towards small peptidic substrates as is the full length ColG. However, this peptidase domain is completely inactive against collagen substrates. Furthermore, it is also shown that full collagenolytic activity is contained in the segment Tyr119-Gly790, the collagenase unit (or collagenase module) of ColG, comprising the activator and peptidase domains
additional information
an activator deletion construct of ColG (Lys396-Lys1118) is fully active towards small peptidic substrates as is the full length ColG. However, this peptidase domain is completely inactive against collagen substrates. Furthermore, it is also shown that full collagenolytic activity is contained in the segment Tyr119-Gly790, the collagenase unit (or collagenase module) of ColG, comprising the activator and peptidase domains
additional information
development of a collagen-like polypeptide-based bone formation system consisting of poly(Pro-Hyp-Gly)10, which mimics the triple helical conformation of collagen, and basic fibroblast growth factor (bFGF) fused to the polycystic kidney disease (PKD) domain and collagen-binding domain (CBD) of Clostridium histolyticum collagenase. The synthetic construct structure is more thermostable (retains structure at up to 80°C) than the native pepsin-soluble bovine type I collagen (loses structure at 50°C). The combination of the collagen binding bFGF fusion protein (bFGF-PKD-CBD) with poly(Pro-Hyp-Gly)10 induces greater bone formation compared to bFGF alone in mice bone fracture models. Method evaluation, overview
additional information
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development of a collagen-like polypeptide-based bone formation system consisting of poly(Pro-Hyp-Gly)10, which mimics the triple helical conformation of collagen, and basic fibroblast growth factor (bFGF) fused to the polycystic kidney disease (PKD) domain and collagen-binding domain (CBD) of Clostridium histolyticum collagenase. The synthetic construct structure is more thermostable (retains structure at up to 80°C) than the native pepsin-soluble bovine type I collagen (loses structure at 50°C). The combination of the collagen binding bFGF fusion protein (bFGF-PKD-CBD) with poly(Pro-Hyp-Gly)10 induces greater bone formation compared to bFGF alone in mice bone fracture models. Method evaluation, overview
additional information
generation of a fusion protein of class II collagenase (ColH) fused to basic fibroblast growth factor (recombinant human bFGF), a potent mitogen for mesenchymal cells that accelerates bone union and repair when applied locally at defect sites. The fusion protein markedly enhances bone formation when loaded onto collagen materials used for grafting (from porcine-derived insoluble type I collagen sheet). Also construction of collagen-binding domain (CBD) and polycystic kidney disease (PKD) domain of Clostridium histolyticum class II collagenase (ColH) fused to bFGF, the fusion protein demonstrates that the fusion protein markedly enhances bone formation when loaded onto collagen materials used for grafting. A fusion protein consisting of parathyroid hormone (PTH) and a CBD is shown to accelerate bone formation in an osteoporosis model more rapidly than treatment with a PTH-PKD-CBD fusion protein after systemic injection. Comparison of the biological properties of two collagen-binding forms of bFGF, bFGF-CBD and bFGF-PKD-CBD. Both fusion proteins promote the in vitro proliferation of periosteal mesenchymal cells, indicating that they have biological activity similar to that of native bFGF. In vivo periosteal bone formation assays in rat femurs showed that both bFGF-CBD and bFGF-PKD-CBD induced periosteal bone formation at higher rates than collagen sheet alone and bFGF. bFGF-PKD-CBD markedly enhances bone formation and has higher collagen-binding ability than bFGF-CBD in in vitro protein release assays
additional information
-
generation of a fusion protein of class II collagenase (ColH) fused to basic fibroblast growth factor (recombinant human bFGF), a potent mitogen for mesenchymal cells that accelerates bone union and repair when applied locally at defect sites. The fusion protein markedly enhances bone formation when loaded onto collagen materials used for grafting (from porcine-derived insoluble type I collagen sheet). Also construction of collagen-binding domain (CBD) and polycystic kidney disease (PKD) domain of Clostridium histolyticum class II collagenase (ColH) fused to bFGF, the fusion protein demonstrates that the fusion protein markedly enhances bone formation when loaded onto collagen materials used for grafting. A fusion protein consisting of parathyroid hormone (PTH) and a CBD is shown to accelerate bone formation in an osteoporosis model more rapidly than treatment with a PTH-PKD-CBD fusion protein after systemic injection. Comparison of the biological properties of two collagen-binding forms of bFGF, bFGF-CBD and bFGF-PKD-CBD. Both fusion proteins promote the in vitro proliferation of periosteal mesenchymal cells, indicating that they have biological activity similar to that of native bFGF. In vivo periosteal bone formation assays in rat femurs showed that both bFGF-CBD and bFGF-PKD-CBD induced periosteal bone formation at higher rates than collagen sheet alone and bFGF. bFGF-PKD-CBD markedly enhances bone formation and has higher collagen-binding ability than bFGF-CBD in in vitro protein release assays
