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evolution
clases of collagenases, overview
evolution
classes of collagenases, overview
evolution
phylogenetic analysis and tree, the enzyme belongs to the peptidase family M9, M09.001. Collagenases structure comparisons, overview. Collagenases structure comparisons, overview. Bacterial collagenases are less specific than those from animal origin. For animal collagenases, the degradation of native triple helical collagen (or water-insoluble native collagen) is crucially dependent on the collagen type and the species of origin. At the contrary, bacterial collagenases can degrade both water-soluble denatured collagens and water-insoluble native molecules
evolution
phylogenetic analysis and tree, the enzyme belongs to the peptidase family M9, M09.003. Collagenases structure comparisons, overview. Collagenases structure comparisons, overview. Bacterial collagenases are less specific than those from animal origin. For animal collagenases, the degradation of native triple helical collagen (or water-insoluble native collagen) is crucially dependent on the collagen type and the species of origin. At the contrary, bacterial collagenases can degrade both water-soluble denatured collagens and water-insoluble native molecules
evolution
phylogenetic analysis and tree, the enzyme belongs to the peptidase family M9, M09.004. Collagenases structure comparisons, overview. Collagenases structure comparisons, overview. Bacterial collagenases are less specific than those from animal origin. For animal collagenases, the degradation of native triple helical collagen (or water-insoluble native collagen) is crucially dependent on the collagen type and the species of origin. At the contrary, bacterial collagenases can degrade both water-soluble denatured collagens and water-insoluble native molecules
evolution
phylogenetic analysis and tree, the enzyme belongs to the peptidase family M9, M09.004. Collagenases structure comparisons, overview. Collagenases structure comparisons, overview. Bacterial collagenases are less specific than those from animal origin. For animal collagenases, the degradation of native triple helical collagen (or water-insoluble native collagen) is crucially dependent on the collagen type and the species of origin. At the contrary, bacterial collagenases can degrade both water-soluble denatured collagens and water-insoluble native molecules
evolution
phylogenetic analysis and tree, the enzyme belongs to the peptidase family M9, subfamily M9A, M09.001. Collagenases structure comparisons, overview. Bacterial collagenases are less specific than those from animal origin. For animal collagenases, the degradation of native triple helical collagen (or water-insoluble native collagen) is crucially dependent on the collagen type and the species of origin. At the contrary, bacterial collagenases can degrade both water-soluble denatured collagens and water-insoluble native molecules
evolution
phylogenetic analysis and tree, the enzyme belongs to the peptidase family M9, subfamily M9A, M09.004. Collagenases structure comparisons, overview. Collagenases structure comparisons, overview. Bacterial collagenases are less specific than those from animal origin. For animal collagenases, the degradation of native triple helical collagen (or water-insoluble native collagen) is crucially dependent on the collagen type and the species of origin. At the contrary, bacterial collagenases can degrade both water-soluble denatured collagens and water-insoluble native molecules
evolution
phylogenetic analysis and tree, the enzyme belongs to the peptidase family M9, subfamily M9B, M09.002. Collagenases structure comparisons, overview. Bacterial collagenases are less specific than those from animal origin. For animal collagenases, the degradation of native triple helical collagen (or water-insoluble native collagen) is crucially dependent on the collagen type and the species of origin. At the contrary, bacterial collagenases can degrade both water-soluble denatured collagens and water-insoluble native molecules
evolution
phylogenetic analysis and tree, the enzyme belongs to the peptidase family M9, subfamily M9B, M09.002. Collagenases structure comparisons, overview. Collagenases structure comparisons, overview. Bacterial collagenases are less specific than those from animal origin. For animal collagenases, the degradation of native triple helical collagen (or water-insoluble native collagen) is crucially dependent on the collagen type and the species of origin. At the contrary, bacterial collagenases can degrade both water-soluble denatured collagens and water-insoluble native molecules
evolution
phylogenetic analysis and tree, the enzyme belongs to the peptidase family M9, subfamily M9B, M09.003. Collagenases structure comparisons, overview. Bacterial collagenases are less specific than those from animal origin. For animal collagenases, the degradation of native triple helical collagen (or water-insoluble native collagen) is crucially dependent on the collagen type and the species of origin. At the contrary, bacterial collagenases can degrade both water-soluble denatured collagens and water-insoluble native molecules
evolution
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phylogenetic analysis and tree, the enzyme belongs to the peptidase family M9, M09.003. Collagenases structure comparisons, overview. Collagenases structure comparisons, overview. Bacterial collagenases are less specific than those from animal origin. For animal collagenases, the degradation of native triple helical collagen (or water-insoluble native collagen) is crucially dependent on the collagen type and the species of origin. At the contrary, bacterial collagenases can degrade both water-soluble denatured collagens and water-insoluble native molecules
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evolution
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phylogenetic analysis and tree, the enzyme belongs to the peptidase family M9, M09.003. Collagenases structure comparisons, overview. Collagenases structure comparisons, overview. Bacterial collagenases are less specific than those from animal origin. For animal collagenases, the degradation of native triple helical collagen (or water-insoluble native collagen) is crucially dependent on the collagen type and the species of origin. At the contrary, bacterial collagenases can degrade both water-soluble denatured collagens and water-insoluble native molecules
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evolution
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phylogenetic analysis and tree, the enzyme belongs to the peptidase family M9, M09.003. Collagenases structure comparisons, overview. Collagenases structure comparisons, overview. Bacterial collagenases are less specific than those from animal origin. For animal collagenases, the degradation of native triple helical collagen (or water-insoluble native collagen) is crucially dependent on the collagen type and the species of origin. At the contrary, bacterial collagenases can degrade both water-soluble denatured collagens and water-insoluble native molecules
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evolution
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phylogenetic analysis and tree, the enzyme belongs to the peptidase family M9, M09.003. Collagenases structure comparisons, overview. Collagenases structure comparisons, overview. Bacterial collagenases are less specific than those from animal origin. For animal collagenases, the degradation of native triple helical collagen (or water-insoluble native collagen) is crucially dependent on the collagen type and the species of origin. At the contrary, bacterial collagenases can degrade both water-soluble denatured collagens and water-insoluble native molecules
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evolution
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phylogenetic analysis and tree, the enzyme belongs to the peptidase family M9, subfamily M9B, M09.002. Collagenases structure comparisons, overview. Collagenases structure comparisons, overview. Bacterial collagenases are less specific than those from animal origin. For animal collagenases, the degradation of native triple helical collagen (or water-insoluble native collagen) is crucially dependent on the collagen type and the species of origin. At the contrary, bacterial collagenases can degrade both water-soluble denatured collagens and water-insoluble native molecules
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evolution
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phylogenetic analysis and tree, the enzyme belongs to the peptidase family M9, M09.003. Collagenases structure comparisons, overview. Collagenases structure comparisons, overview. Bacterial collagenases are less specific than those from animal origin. For animal collagenases, the degradation of native triple helical collagen (or water-insoluble native collagen) is crucially dependent on the collagen type and the species of origin. At the contrary, bacterial collagenases can degrade both water-soluble denatured collagens and water-insoluble native molecules
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evolution
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phylogenetic analysis and tree, the enzyme belongs to the peptidase family M9, subfamily M9B, M09.002. Collagenases structure comparisons, overview. Collagenases structure comparisons, overview. Bacterial collagenases are less specific than those from animal origin. For animal collagenases, the degradation of native triple helical collagen (or water-insoluble native collagen) is crucially dependent on the collagen type and the species of origin. At the contrary, bacterial collagenases can degrade both water-soluble denatured collagens and water-insoluble native molecules
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evolution
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phylogenetic analysis and tree, the enzyme belongs to the peptidase family M9, M09.003. Collagenases structure comparisons, overview. Collagenases structure comparisons, overview. Bacterial collagenases are less specific than those from animal origin. For animal collagenases, the degradation of native triple helical collagen (or water-insoluble native collagen) is crucially dependent on the collagen type and the species of origin. At the contrary, bacterial collagenases can degrade both water-soluble denatured collagens and water-insoluble native molecules
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evolution
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phylogenetic analysis and tree, the enzyme belongs to the peptidase family M9, M09.004. Collagenases structure comparisons, overview. Collagenases structure comparisons, overview. Bacterial collagenases are less specific than those from animal origin. For animal collagenases, the degradation of native triple helical collagen (or water-insoluble native collagen) is crucially dependent on the collagen type and the species of origin. At the contrary, bacterial collagenases can degrade both water-soluble denatured collagens and water-insoluble native molecules
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evolution
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phylogenetic analysis and tree, the enzyme belongs to the peptidase family M9, M09.003. Collagenases structure comparisons, overview. Collagenases structure comparisons, overview. Bacterial collagenases are less specific than those from animal origin. For animal collagenases, the degradation of native triple helical collagen (or water-insoluble native collagen) is crucially dependent on the collagen type and the species of origin. At the contrary, bacterial collagenases can degrade both water-soluble denatured collagens and water-insoluble native molecules
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evolution
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phylogenetic analysis and tree, the enzyme belongs to the peptidase family M9, M09.001. Collagenases structure comparisons, overview. Collagenases structure comparisons, overview. Bacterial collagenases are less specific than those from animal origin. For animal collagenases, the degradation of native triple helical collagen (or water-insoluble native collagen) is crucially dependent on the collagen type and the species of origin. At the contrary, bacterial collagenases can degrade both water-soluble denatured collagens and water-insoluble native molecules
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evolution
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phylogenetic analysis and tree, the enzyme belongs to the peptidase family M9, M09.003. Collagenases structure comparisons, overview. Collagenases structure comparisons, overview. Bacterial collagenases are less specific than those from animal origin. For animal collagenases, the degradation of native triple helical collagen (or water-insoluble native collagen) is crucially dependent on the collagen type and the species of origin. At the contrary, bacterial collagenases can degrade both water-soluble denatured collagens and water-insoluble native molecules
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evolution
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phylogenetic analysis and tree, the enzyme belongs to the peptidase family M9, M09.004. Collagenases structure comparisons, overview. Collagenases structure comparisons, overview. Bacterial collagenases are less specific than those from animal origin. For animal collagenases, the degradation of native triple helical collagen (or water-insoluble native collagen) is crucially dependent on the collagen type and the species of origin. At the contrary, bacterial collagenases can degrade both water-soluble denatured collagens and water-insoluble native molecules
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malfunction
a Clostridium perfringens null-mutant of colA is still able to cause disease
malfunction
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a Clostridium perfringens null-mutant of colA is still able to cause disease
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malfunction
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a Clostridium perfringens null-mutant of colA is still able to cause disease
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physiological function
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ColB is an important virulence factor required for Bacillis thuringiensis infecting Caenorhabditis elegans. The enzyme highly important for destruction of the intestine thereby facilitates the adaptation and colonization of Bacillus thuringiensis in Caenorhabditis elegans
physiological function
collagenases (class I and class II clostridial collagenases expressed by colG and colH genes, respectively) are able to digest both type I and type III collagen, acting in a complementary and synergistic manner
physiological function
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the bacterial collagenase affects the extracellular matrix (ECM) in the lungs of C57BL/6 mice. Mechanical loading increases the effects of enzyme activity characterized by an irreversible decline in stiffness and tissue deterioration. Physiological levels of mechanical forces are capable of modifying the activity of collagenase, a key remodeling enzyme of the ECM. Role of collagen degradation in general tissue remodeling and disease progression, overview
physiological function
the collagenase A produced by Clostridium perfringens seems to be involved in tissue necrosis
physiological function
the enzyme is involved in collagen degradation. Type I collagenase ColG acts on the N-terminal level of the triple helix of collagen. This first step is followed by the loosening of the C-terminal structure of the enzyme converting the collagen as a gelatinase and degradation of the interstitial collagen obtaining little oligopeptides
physiological function
the enzyme is involved in collagen degradation. Type II collagenase ColH acts inside of the collagen triple helix molecule. This first step is followed by the loosening of the C-terminal structure of the enzyme converting the collagen as a gelatinase and degradation of the interstitial collagen obtaining little oligopeptides
physiological function
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the collagenase A produced by Clostridium perfringens seems to be involved in tissue necrosis
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physiological function
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the collagenase A produced by Clostridium perfringens seems to be involved in tissue necrosis
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physiological function
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ColB is an important virulence factor required for Bacillis thuringiensis infecting Caenorhabditis elegans. The enzyme highly important for destruction of the intestine thereby facilitates the adaptation and colonization of Bacillus thuringiensis in Caenorhabditis elegans
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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
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
additional information
mechanism of action of collagenase clostridium histolyticum for clinical application. Residues Glu446 and Glu451 of the S3 segment are responsible for the catalysis through interaction with the residues of His linked to Zn2+, forming two triads Glu446-His419-Zn2+ and Glu451-His415-Zn2+, which play a critical role in the catalytic mechanism of ColH
additional information
mechanism of action of collagenase clostridium histolyticum for clinical application. Residues Glu446 and Glu451 of the S3 segment are responsible for the catalysis through interaction with the residues of His linked to Zn2+, forming two triads Glu446-His419-Zn2+ and Glu451-His415-Zn2+, which play a critical role in the catalytic mechanism of ColH
additional information
mechanism of action of collagenase clostridium histolyticum for clinical application. The action of ColG is done in intermediate areas of the collagen triple helix. Structure-function relationship, overview
additional information
mechanism of action of collagenase clostridium histolyticum for clinical application. The action of ColG is done in intermediate areas of the collagen triple helix. Structure-function relationship, overview
additional information
prior to collagenolysis, ColG follows a two-step mechanism similar to MMPs, in which unrolling collagen (micro)fibrils and unwinding the triple-helical collagen are prerequisites for cleavage. Construction a full-length structural model of ColG, collagenase G can switch between opened and closed states. In the closed state, the triple-helical collagen acts as a source of attraction between both domains of the collagenase module (the activator and the peptidase domain). ColG collagenolysis mechanism, overview
additional information
prior to collagenolysis, ColG follows a two-step mechanism similar to MMPs, in which unrolling collagen (micro)fibrils and unwinding the triple-helical collagen are prerequisites for cleavage. Construction a full-length structural model of ColG, collagenase G can switch between opened and closed states. In the closed state, the triple-helical collagen acts as a source of attraction between both domains of the collagenase module (the activator and the peptidase domain). ColG collagenolysis mechanism, overview
additional information
the S1 domain is the catalytic segment containing the sequence HEXXH, a group of amino acids that constitute the catalytic center. The S3 domain is the segment where the collagen-binding takes place. The S2a and S2b segments are the segments between domains. Enzyme domain structure, overview
additional information
the S1 domain is the catalytic segment containing the sequence HEXXH, a group of amino acids that constitute the catalytic center. The S3 domain is the segment where the collagen-binding takes place. The S2a and S2b segments are the segments between domains. Enzyme domain structure, overview