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Literature summary for 3.4.24.3 extracted from
- Bacterial collagenases - a review (2016), Crit. Rev. Microbiol., 42, 106-126 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene colG | Hathewaya histolytica |
| gene colH | Hathewaya histolytica |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystal structure determination and analysis | Hathewaya histolytica |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| 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 | Hathewaya histolytica |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | a zinc metalloproteinase | Hathewaya histolytica |  |
| Zn2+ | a zinc metalloproteinase | Vibrio alginolyticus | |
| Zn2+ | a zinc metalloproteinase | Vibrio mimicus | |
| Zn2+ | a zinc metalloproteinase | Vibrio cholerae serotype O1 | |
| Zn2+ | a zinc metalloproteinase | Vibrio parahaemolyticus RIMD 2210633 | |
| Zn2+ | a zinc metalloproteinase | Vibrio parahaemolyticus | |
| Zn2+ | a zinc metalloproteinase | Bacillus cereus | |
| Zn2+ | a zinc metalloproteinase | Clostridium perfringens | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 120000 | - |
- |
Clostridium perfringens |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Collagen + H2O | Vibrio alginolyticus | - |
? | - |
? | |
| Collagen + H2O | Vibrio mimicus | - |
? | - |
? | |
| Collagen + H2O | Vibrio cholerae serotype O1 | - |
? | - |
? | |
| Collagen + H2O | Vibrio parahaemolyticus RIMD 2210633 | - |
? | - |
? | |
| Collagen + H2O | Vibrio parahaemolyticus | - |
? | - |
? | |
| Collagen + H2O | Bacillus cereus | - |
? | - |
? | |
| Collagen + H2O | Clostridium perfringens | - |
? | - |
? | |
| Collagen + H2O | Bacillus cereus ATCC 14579 | - |
? | - |
? | |
| Collagen + H2O | Bacillus cereus NRRL B-3711 | - |
? | - |
? | |
| Collagen + H2O | Bacillus cereus NCIMB 9373 | - |
? | - |
? | |
| Collagen + H2O | Bacillus cereus DSM 31 | - |
? | - |
? | |
| Collagen + H2O | Clostridium perfringens type A | - |
? | - |
? | |
| Collagen + H2O | Bacillus cereus NBRC 15305 | - |
? | - |
? | |
| Collagen + H2O | Clostridium perfringens 13 | - |
? | - |
? | |
| Collagen + H2O | Bacillus cereus ZK | - |
? | - |
? | |
| Collagen + H2O | Vibrio cholerae serotype O1 El Tor Inaba N16961 | - |
? | - |
? | |
| Collagen + H2O | Bacillus cereus JCM 2152 | - |
? | - |
? | |
| Collagen + H2O | Vibrio parahaemolyticus 04 | - |
? | - |
? | |
| Collagen + H2O | Bacillus cereus E33L | - |
? | - |
? | |
| Collagen + H2O | Vibrio cholerae serotype O1 ATCC 39315 | - |
? | - |
? | |
| Collagen type I + H2O | Hathewaya histolytica | - |
? | - |
? | |
| Collagen type III + H2O | Hathewaya histolytica | - |
? | - |
? | |
| Gelatin + H2O | Clostridium perfringens | - |
? | - |
? | |
| Gelatin + H2O | Clostridium perfringens type A | - |
? | - |
? | |
| Gelatin + H2O | Clostridium perfringens 13 | - |
? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus cereus | Q4V1V2 | - |
- |
| Bacillus cereus | Q81DA6 | - |
- |
| Bacillus cereus ATCC 14579 | Q81DA6 | - |
- |
| Bacillus cereus DSM 31 | Q81DA6 | - |
- |
| Bacillus cereus E33L | Q4V1V2 | - |
- |
| Bacillus cereus JCM 2152 | Q81DA6 | - |
- |
| Bacillus cereus NBRC 15305 | Q81DA6 | - |
- |
| Bacillus cereus NCIMB 9373 | Q81DA6 | - |
- |
| Bacillus cereus NRRL B-3711 | Q81DA6 | - |
- |
| Bacillus cereus ZK | Q4V1V2 | - |
- |
| Clostridium perfringens | P43153 | - |
- |
| Clostridium perfringens 13 | P43153 | - |
- |
| Clostridium perfringens type A | P43153 | - |
- |
| Hathewaya histolytica | Q46085 | - |
- |
| Hathewaya histolytica | Q9X721 | - |
- |
| Vibrio alginolyticus | P43154 | - |
- |
| Vibrio cholerae serotype O1 | Q9KRJ0 | - |
- |
| Vibrio cholerae serotype O1 ATCC 39315 | Q9KRJ0 | - |
- |
| Vibrio cholerae serotype O1 El Tor Inaba N16961 | Q9KRJ0 | - |
- |
| Vibrio mimicus | O67990 | - |
- |
| Vibrio parahaemolyticus | Q9AMB9 | - |
- |
| Vibrio parahaemolyticus 04 | Q9AMB9 | - |
- |
| Vibrio parahaemolyticus RIMD 2210633 | Q56696 | serotype O3:K6 | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Collagen + H2O | - |
Vibrio alginolyticus | ? | - |
? | |
| Collagen + H2O | - |
Vibrio mimicus | ? | - |
? | |
| Collagen + H2O | - |
Vibrio cholerae serotype O1 | ? | - |
? | |
| Collagen + H2O | - |
Vibrio parahaemolyticus RIMD 2210633 | ? | - |
? | |
| Collagen + H2O | - |
Vibrio parahaemolyticus | ? | - |
? | |
| Collagen + H2O | - |
Bacillus cereus | ? | - |
? | |
| Collagen + H2O | - |
Clostridium perfringens | ? | - |
? | |
| Collagen + H2O | - |
Bacillus cereus ATCC 14579 | ? | - |
? | |
| Collagen + H2O | - |
Bacillus cereus NRRL B-3711 | ? | - |
? | |
| Collagen + H2O | - |
Bacillus cereus NCIMB 9373 | ? | - |
? | |
| Collagen + H2O | - |
Bacillus cereus DSM 31 | ? | - |
? | |
| Collagen + H2O | - |
Clostridium perfringens type A | ? | - |
? | |
| Collagen + H2O | - |
Bacillus cereus NBRC 15305 | ? | - |
? | |
| Collagen + H2O | - |
Clostridium perfringens 13 | ? | - |
? | |
| Collagen + H2O | - |
Bacillus cereus ZK | ? | - |
? | |
| Collagen + H2O | - |
Vibrio cholerae serotype O1 El Tor Inaba N16961 | ? | - |
? | |
| Collagen + H2O | - |
Bacillus cereus JCM 2152 | ? | - |
? | |
| Collagen + H2O | - |
Vibrio parahaemolyticus 04 | ? | - |
? | |
| Collagen + H2O | - |
Bacillus cereus E33L | ? | - |
? | |
| Collagen + H2O | - |
Vibrio cholerae serotype O1 ATCC 39315 | ? | - |
? | |
| Collagen type I + H2O | - |
Hathewaya histolytica | ? | - |
? | |
| Collagen type III + H2O | - |
Hathewaya histolytica | ? | - |
? | |
| Gelatin + H2O | - |
Clostridium perfringens | ? | - |
? | |
| Gelatin + H2O | - |
Clostridium perfringens type A | ? | - |
? | |
| Gelatin + H2O | - |
Clostridium perfringens 13 | ? | - |
? | |
| additional information | ColG can process collagen microfibrils | Hathewaya histolytica | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | enzyme domain structure, overview | Bacillus cereus |
| More | enzyme domain structure, overview. Enzyme ColA possesses segments S1, S2, S3a, and S3b. In ColA, S3 is composed by a tandem repeated structure (S3a and S3b) that enhances binding to collagen, this is characteristic of class I collagenases | Clostridium perfringens |
| More | enzyme domain structure, overview. Enzyme ColH possesses segments S1, S2a, S2b, and S3 | Hathewaya histolytica |
| More | enzyme domain structure, overview. In ColG, S3 is composed by a tandem repeated structure (S3a and S3b) that enhances binding to collagen, this is characteristic of class I collagenases. ColG functional domains: (i) the CBD(s) that locate and anchor the enzyme to collagen by specifically recognizing their triplehelical conformation. ColG CBDs promote interaction with fibrils, not with individual triple helices; (ii) the PKD-like domain(s) swell and prepare the substrate without triple helix unwinding; and (iii) the collagenase unit degrades the prepared collagen molecules, digesting them from microfibrils of 35A diameter downwards | Hathewaya histolytica |
| More | enzyme domain structure, overview. In peptidases from subfamily type M09.004, the PKD-like domain and the bacterial PPC are absent, resulting in lower molecular mass enzymes | Vibrio mimicus |
| More | enzyme domain structure, overview. In peptidases from subfamily type M09.004, the PKD-like domain and the bacterial PPC are absent, resulting in lower molecular mass enzymes | Vibrio cholerae serotype O1 |
| More | enzyme domain structure, overview. In peptidases from subfamily type M09.004, the PKD-like domain and the bacterial PPC are absent, resulting in lower molecular mass enzymes | Vibrio parahaemolyticus RIMD 2210633 |
| More | enzyme domain structure, overview. M09.001 enzymes exhibit a peptidase M9N domain, a peptidase M9 domain, a PKD-like domain and/or a bacterial pre-peptidase C-terminal domain (PPC) | Vibrio alginolyticus |
| More | enzyme domain structure, overview. M09.001 enzymes exhibit a peptidase M9N domain, a peptidase M9 domain, a PKD-like domain and/or a bacterial pre-peptidase C-terminal domain (PPC) | Vibrio parahaemolyticus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| bacterial collagenase | - |
Hathewaya histolytica |
| bacterial collagenase | - |
Vibrio alginolyticus |
| bacterial collagenase | - |
Vibrio mimicus |
| bacterial collagenase | - |
Vibrio cholerae serotype O1 |
| bacterial collagenase | - |
Vibrio parahaemolyticus RIMD 2210633 |
| bacterial collagenase | - |
Vibrio parahaemolyticus |
| bacterial collagenase | - |
Bacillus cereus |
| bacterial collagenase | - |
Clostridium perfringens |
| bacterial collagenase V | - |
Vibrio alginolyticus |
| BC_2466 | - |
Bacillus cereus |
| class I collagenase | - |
Hathewaya histolytica |
| class I collagenase | - |
Clostridium perfringens |
| class II collagenase | - |
Hathewaya histolytica |
| class II collagenase | - |
Vibrio mimicus |
| class II collagenase | - |
Vibrio cholerae serotype O1 |
| class II collagenase | - |
Vibrio parahaemolyticus RIMD 2210633 |
| class II collagenase | - |
Bacillus cereus |
| class III collagenase | - |
Vibrio alginolyticus |
| class III collagenase | - |
Vibrio parahaemolyticus |
| ColA | - |
Vibrio alginolyticus |
| ColA | - |
Vibrio cholerae serotype O1 |
| ColA | - |
Vibrio parahaemolyticus RIMD 2210633 |
| ColA | - |
Bacillus cereus |
| ColA | - |
Clostridium perfringens |
| ColG | - |
Hathewaya histolytica |
| ColH | - |
Hathewaya histolytica |
| collagenase G | - |
Hathewaya histolytica |
| collagenase H | - |
Hathewaya histolytica |
| M9-peptidase | - |
Hathewaya histolytica |
| M9-peptidase | - |
Vibrio alginolyticus |
| M9-peptidase | - |
Vibrio mimicus |
| M9-peptidase | - |
Vibrio cholerae serotype O1 |
| M9-peptidase | - |
Vibrio parahaemolyticus RIMD 2210633 |
| M9-peptidase | - |
Vibrio parahaemolyticus |
| M9-peptidase | - |
Bacillus cereus |
| M9-peptidase | - |
Clostridium perfringens |
| microbial collagenase | - |
Hathewaya histolytica |
| microbial collagenase | - |
Vibrio alginolyticus |
| microbial collagenase | - |
Vibrio mimicus |
| microbial collagenase | - |
Vibrio cholerae serotype O1 |
| microbial collagenase | - |
Vibrio parahaemolyticus RIMD 2210633 |
| microbial collagenase | - |
Vibrio parahaemolyticus |
| microbial collagenase | - |
Bacillus cereus |
| microbial collagenase | - |
Clostridium perfringens |
| VMC peptidase | - |
Vibrio mimicus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 | Vibrio parahaemolyticus |
| 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 | Bacillus cereus |
| 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 | Vibrio cholerae serotype O1 |
| 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 | Vibrio parahaemolyticus RIMD 2210633 |
| 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 | Vibrio alginolyticus |
| 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 | Vibrio mimicus |
| 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 | Hathewaya histolytica |
| 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 | Clostridium perfringens |
| 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 | Hathewaya histolytica |
| malfunction | a Clostridium perfringens null-mutant of colA is still able to cause disease | Clostridium perfringens |
| 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 | Hathewaya histolytica |
| 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 | Hathewaya histolytica |
| physiological function | the collagenase A produced by Clostridium perfringens seems to be involved in tissue necrosis | Clostridium perfringens |
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