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
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3.4.24.3 microbial collagenaseAdvanced search results
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Natural Substrates Products on EC 3.4.24.3 - microbial collagenase
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Collagen + H2O
?
Clostridium capitorale
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degradation of helical regions of native collagen to small fragments, preferential cleavage: -Gly in the sequence Pro-Xaa-Gly-Pro
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-
?
Collagen + H2O
?
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degradation of helical regions of native collagen to small fragments, preferential cleavage: -Gly in the sequence Pro-Xaa-Gly-Pro
-
-
?
Collagen + H2O
?
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clostridial collagenase A is effective in degrading collagen in eschar tissue and promoting healing in partial-thickness burns, CCA aggravates the systemic inflammatory response in rats with partial-thickness burns, inflammatory reactions such as fever, leukocytosis or leukocytopenia and increased CRP levels in sera are often observed in a significant proportion of burn victims treated with CCA ointment, although synchronous wound swab cultures show no signs of infection, overview
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-
?
Collagen + H2O
?
Clostridium welchii
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degradation of helical regions of native collagen to small fragments, preferential cleavage: -Gly in the sequence Pro-Xaa-Gly-Pro
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-
?
Collagen + H2O
?
-
degradation of helical regions of native collagen to small fragments, preferential cleavage: -Gly in the sequence Pro-Xaa-Gly-Pro
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-
?
Collagen + H2O
?
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proteolytic degradation, the enzyme helps the skin to heal after burns and dermal ulcers, but can cause allergic reactions, overview
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-
?
Collagen + H2O
?
type II collagenase ColH acts inside of the collagen triple helix molecule
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-
?
Collagen + H2O
?
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degradation of helical regions of native collagen to small fragments, preferential cleavage: -Gly in the sequence Pro-Xaa-Gly-Pro
-
-
?
Collagen + H2O
?
-
degradation of helical regions of native collagen to small fragments, preferential cleavage: -Gly in the sequence Pro-Xaa-Gly-Pro
-
-
?
Collagen + H2O
?
-
degradation of helical regions of native collagen to small fragments, preferential cleavage: -Gly in the sequence Pro-Xaa-Gly-Pro
-
-
?
Collagen + H2O
?
-
degradation of helical regions of native collagen to small fragments, preferential cleavage: -Gly in the sequence Pro-Xaa-Gly-Pro
-
-
?
Collagen + H2O
?
-
degradation of helical regions of native collagen to small fragments, preferential cleavage: -Gly in the sequence Pro-Xaa-Gly-Pro
-
-
?
Collagen + H2O
?
-
degradation of helical regions of native collagen to small fragments, preferential cleavage: -Gly in the sequence Pro-Xaa-Gly-Pro
-
-
?
Collagen + H2O
?
-
degradation of helical regions of native collagen to small fragments, preferential cleavage: -Gly in the sequence Pro-Xaa-Gly-Pro
-
-
?
Collagen + H2O
?
-
degradation of helical regions of native collagen to small fragments, preferential cleavage: -Gly in the sequence Pro-Xaa-Gly-Pro
-
-
?
Collagen type I + H2O
?
type I collagenase ColG acts on the N-terminal level of the triple helix of collagen
-
-
?
additional information
?
-
-
human dentin surfaces bonded to adhesive material in teeth repair are sensitive to aging, microtensile bond strength values are affected by different adhesives, specimen sizes and storing periods, but not by the presence or absence of bacterial collagenase, overview
-
-
?
additional information
?
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ColG moves about 14.5 nm toward the collagen N-terminus in 3.8 s in a manner dependent on a catalytic zinc ion. While ColG is engaged, the collagen molecules are not only degraded but also occasionally rearranged to thicken neighboring collagen fibrils, relationship between collagen structure and collagenase movement, detailed overview. Collagen molecules form self-assembled thin sheets characterized by D-bands, also known as collagen microribbons, on a mica surface in the presence of 0.2 M potassium. ColG clears the collagen microribbon from the lateral edge, rather than from the middle. Strongly polarized movement of ColG on collagen fibrils
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-
?
additional information
?
-
-
ColG moves about 14.5 nm toward the collagen N-terminus in 3.8 s in a manner dependent on a catalytic zinc ion. While ColG is engaged, the collagen molecules are not only degraded but also occasionally rearranged to thicken neighboring collagen fibrils, relationship between collagen structure and collagenase movement, detailed overview. Collagen molecules form self-assembled thin sheets characterized by D-bands, also known as collagen microribbons, on a mica surface in the presence of 0.2 M potassium. ColG clears the collagen microribbon from the lateral edge, rather than from the middle. Strongly polarized movement of ColG on collagen fibrils
-
-
?
additional information
?
-
-
collagenase is capable of eliciting a variety of tissue responses in mice depending upon its route of administration. Intranasal instillation results in confluent pulmonary hemorrhage, intraperitoneal injections result in severe abdominal hemorrhage with foci in the intestinal serosa. Intravenous injections elicit abdominal hemorrhage and petichial hemorrhage with focal necrosis of the lungs, subcutaneous injections result in necrotic, ulcerating lesions
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?
