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Literature summary extracted from

  • Duarte, A.; Correia, A.; Esteves, A.
    Bacterial collagenases - a review (2016), Crit. Rev. Microbiol., 42, 106-126 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.24.3 gene colG Hathewaya histolytica
3.4.24.3 gene colH Hathewaya histolytica

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.24.3 crystal structure determination and analysis Hathewaya histolytica

Protein Variants

EC Number Protein Variants Comment Organism
3.4.24.3 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

EC Number Metals/Ions Comment Organism Structure
3.4.24.3 Zn2+ a zinc metalloproteinase Hathewaya histolytica
3.4.24.3 Zn2+ a zinc metalloproteinase Vibrio alginolyticus
3.4.24.3 Zn2+ a zinc metalloproteinase Vibrio mimicus
3.4.24.3 Zn2+ a zinc metalloproteinase Vibrio cholerae serotype O1
3.4.24.3 Zn2+ a zinc metalloproteinase Vibrio parahaemolyticus RIMD 2210633
3.4.24.3 Zn2+ a zinc metalloproteinase Vibrio parahaemolyticus
3.4.24.3 Zn2+ a zinc metalloproteinase Bacillus cereus
3.4.24.3 Zn2+ a zinc metalloproteinase Clostridium perfringens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.24.3 120000
-
-
 Clostridium perfringens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.24.3 Collagen + H2O Vibrio alginolyticus
-
 ?
-
 ?
3.4.24.3 Collagen + H2O Vibrio mimicus
-
 ?
-
 ?
3.4.24.3 Collagen + H2O Vibrio cholerae serotype O1
-
 ?
-
 ?
3.4.24.3 Collagen + H2O Vibrio parahaemolyticus RIMD 2210633
-
 ?
-
 ?
3.4.24.3 Collagen + H2O Vibrio parahaemolyticus
-
 ?
-
 ?
3.4.24.3 Collagen + H2O Bacillus cereus
-
 ?
-
 ?
3.4.24.3 Collagen + H2O Clostridium perfringens
-
 ?
-
 ?
3.4.24.3 Collagen + H2O Bacillus cereus ATCC 14579
-
 ?
-
 ?
3.4.24.3 Collagen + H2O Bacillus cereus NRRL B-3711
-
 ?
-
 ?
3.4.24.3 Collagen + H2O Bacillus cereus NCIMB 9373
-
 ?
-
 ?
3.4.24.3 Collagen + H2O Bacillus cereus DSM 31
-
 ?
-
 ?
3.4.24.3 Collagen + H2O Clostridium perfringens type A
-
 ?
-
 ?
3.4.24.3 Collagen + H2O Bacillus cereus NBRC 15305
-
 ?
-
 ?
3.4.24.3 Collagen + H2O Clostridium perfringens 13
-
 ?
-
 ?
3.4.24.3 Collagen + H2O Bacillus cereus ZK
-
 ?
-
 ?
3.4.24.3 Collagen + H2O Vibrio cholerae serotype O1 El Tor Inaba N16961
-
 ?
-
 ?
3.4.24.3 Collagen + H2O Bacillus cereus JCM 2152
-
 ?
-
 ?
3.4.24.3 Collagen + H2O Vibrio parahaemolyticus 04
-
 ?
-
 ?
3.4.24.3 Collagen + H2O Bacillus cereus E33L
-
 ?
-
 ?
3.4.24.3 Collagen + H2O Vibrio cholerae serotype O1 ATCC 39315
-
 ?
-
 ?
3.4.24.3 Collagen type I + H2O Hathewaya histolytica
-
 ?
-
 ?
3.4.24.3 Collagen type III + H2O Hathewaya histolytica
-
 ?
-
 ?
3.4.24.3 Gelatin + H2O Clostridium perfringens
-
 ?
-
 ?
3.4.24.3 Gelatin + H2O Clostridium perfringens type A
-
 ?
-
 ?
3.4.24.3 Gelatin + H2O Clostridium perfringens 13
-
 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.3 Bacillus cereus Q4V1V2
-
-
3.4.24.3 Bacillus cereus Q81DA6
-
-
3.4.24.3 Bacillus cereus ATCC 14579 Q81DA6
-
-
3.4.24.3 Bacillus cereus DSM 31 Q81DA6
-
-
3.4.24.3 Bacillus cereus E33L Q4V1V2
-
-
3.4.24.3 Bacillus cereus JCM 2152 Q81DA6
-
-
3.4.24.3 Bacillus cereus NBRC 15305 Q81DA6
-
-
3.4.24.3 Bacillus cereus NCIMB 9373 Q81DA6
-
-
3.4.24.3 Bacillus cereus NRRL B-3711 Q81DA6
-
-
3.4.24.3 Bacillus cereus ZK Q4V1V2
-
-
3.4.24.3 Clostridium perfringens P43153
-
-
3.4.24.3 Clostridium perfringens 13 P43153
-
-
3.4.24.3 Clostridium perfringens type A P43153
-
-
3.4.24.3 Hathewaya histolytica Q46085
-
-
3.4.24.3 Hathewaya histolytica Q9X721
-
-
3.4.24.3 Vibrio alginolyticus P43154
-
-
3.4.24.3 Vibrio cholerae serotype O1 Q9KRJ0
-
-
3.4.24.3 Vibrio cholerae serotype O1 ATCC 39315 Q9KRJ0
-
-
3.4.24.3 Vibrio cholerae serotype O1 El Tor Inaba N16961 Q9KRJ0
-
-
3.4.24.3 Vibrio mimicus O67990
-
-
3.4.24.3 Vibrio parahaemolyticus Q9AMB9
-
-
3.4.24.3 Vibrio parahaemolyticus 04 Q9AMB9
-
-
3.4.24.3 Vibrio parahaemolyticus RIMD 2210633 Q56696 serotype O3:K6
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.3 Collagen + H2O
-
 Vibrio alginolyticus ?
-
 ?
3.4.24.3 Collagen + H2O
-
 Vibrio mimicus ?
-
 ?
3.4.24.3 Collagen + H2O
-
 Vibrio cholerae serotype O1 ?
-
 ?
3.4.24.3 Collagen + H2O
-
 Vibrio parahaemolyticus RIMD 2210633 ?
-
 ?
3.4.24.3 Collagen + H2O
-
 Vibrio parahaemolyticus ?
-
 ?
3.4.24.3 Collagen + H2O
-
 Bacillus cereus ?
-
 ?
3.4.24.3 Collagen + H2O
-
 Clostridium perfringens ?
-
 ?
3.4.24.3 Collagen + H2O
-
 Bacillus cereus ATCC 14579 ?
-
 ?
3.4.24.3 Collagen + H2O
-
 Bacillus cereus NRRL B-3711 ?
-
 ?
3.4.24.3 Collagen + H2O
-
 Bacillus cereus NCIMB 9373 ?
-
 ?
3.4.24.3 Collagen + H2O
-
 Bacillus cereus DSM 31 ?
-
 ?
3.4.24.3 Collagen + H2O
-
 Clostridium perfringens type A ?
-
 ?
3.4.24.3 Collagen + H2O
-
 Bacillus cereus NBRC 15305 ?
-
 ?
3.4.24.3 Collagen + H2O
-
 Clostridium perfringens 13 ?
-
 ?
3.4.24.3 Collagen + H2O
-
 Bacillus cereus ZK ?
-
 ?
3.4.24.3 Collagen + H2O
-
 Vibrio cholerae serotype O1 El Tor Inaba N16961 ?
-
 ?
3.4.24.3 Collagen + H2O
-
 Bacillus cereus JCM 2152 ?
-
 ?
3.4.24.3 Collagen + H2O
-
 Vibrio parahaemolyticus 04 ?
-
 ?
3.4.24.3 Collagen + H2O
-
 Bacillus cereus E33L ?
-
 ?
3.4.24.3 Collagen + H2O
-
 Vibrio cholerae serotype O1 ATCC 39315 ?
-
 ?
3.4.24.3 Collagen type I + H2O
-
 Hathewaya histolytica ?
-
 ?
3.4.24.3 Collagen type III + H2O
-
 Hathewaya histolytica ?
-
 ?
3.4.24.3 Gelatin + H2O
-
 Clostridium perfringens ?
-
 ?
3.4.24.3 Gelatin + H2O
-
 Clostridium perfringens type A ?
-
 ?
3.4.24.3 Gelatin + H2O
-
 Clostridium perfringens 13 ?
-
 ?
3.4.24.3 additional information ColG can process collagen microfibrils Hathewaya histolytica ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.24.3 More enzyme domain structure, overview Bacillus cereus
3.4.24.3 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
3.4.24.3 More enzyme domain structure, overview. Enzyme ColH possesses segments S1, S2a, S2b, and S3 Hathewaya histolytica
3.4.24.3 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
3.4.24.3 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
3.4.24.3 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
3.4.24.3 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
3.4.24.3 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
3.4.24.3 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

EC Number Synonyms Comment Organism
3.4.24.3 bacterial collagenase
-
 Hathewaya histolytica
3.4.24.3 bacterial collagenase
-
 Vibrio alginolyticus
3.4.24.3 bacterial collagenase
-
 Vibrio mimicus
3.4.24.3 bacterial collagenase
-
 Vibrio cholerae serotype O1
3.4.24.3 bacterial collagenase
-
 Vibrio parahaemolyticus RIMD 2210633
3.4.24.3 bacterial collagenase
-
 Vibrio parahaemolyticus
3.4.24.3 bacterial collagenase
-
 Bacillus cereus
3.4.24.3 bacterial collagenase
-
 Clostridium perfringens
3.4.24.3 bacterial collagenase V
-
 Vibrio alginolyticus
3.4.24.3 BC_2466
-
 Bacillus cereus
3.4.24.3 class I collagenase
-
 Hathewaya histolytica
3.4.24.3 class I collagenase
-
 Clostridium perfringens
3.4.24.3 class II collagenase
-
 Hathewaya histolytica
3.4.24.3 class II collagenase
-
 Vibrio mimicus
3.4.24.3 class II collagenase
-
 Vibrio cholerae serotype O1
3.4.24.3 class II collagenase
-
 Vibrio parahaemolyticus RIMD 2210633
3.4.24.3 class II collagenase
-
 Bacillus cereus
3.4.24.3 class III collagenase
-
 Vibrio alginolyticus
3.4.24.3 class III collagenase
-
 Vibrio parahaemolyticus
3.4.24.3 ColA
-
 Vibrio alginolyticus
3.4.24.3 ColA
-
 Vibrio cholerae serotype O1
3.4.24.3 ColA
-
 Vibrio parahaemolyticus RIMD 2210633
3.4.24.3 ColA
-
 Bacillus cereus
3.4.24.3 ColA
-
 Clostridium perfringens
3.4.24.3 ColG
-
 Hathewaya histolytica
3.4.24.3 ColH
-
 Hathewaya histolytica
3.4.24.3 collagenase G
-
 Hathewaya histolytica
3.4.24.3 collagenase H
-
 Hathewaya histolytica
3.4.24.3 M9-peptidase
-
 Hathewaya histolytica
3.4.24.3 M9-peptidase
-
 Vibrio alginolyticus
3.4.24.3 M9-peptidase
-
 Vibrio mimicus
3.4.24.3 M9-peptidase
-
 Vibrio cholerae serotype O1
3.4.24.3 M9-peptidase
-
 Vibrio parahaemolyticus RIMD 2210633
3.4.24.3 M9-peptidase
-
 Vibrio parahaemolyticus
3.4.24.3 M9-peptidase
-
 Bacillus cereus
3.4.24.3 M9-peptidase
-
 Clostridium perfringens
3.4.24.3 microbial collagenase
-
 Hathewaya histolytica
3.4.24.3 microbial collagenase
-
 Vibrio alginolyticus
3.4.24.3 microbial collagenase
-
 Vibrio mimicus
3.4.24.3 microbial collagenase
-
 Vibrio cholerae serotype O1
3.4.24.3 microbial collagenase
-
 Vibrio parahaemolyticus RIMD 2210633
3.4.24.3 microbial collagenase
-
 Vibrio parahaemolyticus
3.4.24.3 microbial collagenase
-
 Bacillus cereus
3.4.24.3 microbial collagenase
-
 Clostridium perfringens
3.4.24.3 VMC peptidase
-
 Vibrio mimicus

General Information

EC Number General Information Comment Organism
3.4.24.3 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
3.4.24.3 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
3.4.24.3 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
3.4.24.3 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
3.4.24.3 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
3.4.24.3 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
3.4.24.3 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
3.4.24.3 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
3.4.24.3 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
3.4.24.3 malfunction a Clostridium perfringens null-mutant of colA is still able to cause disease Clostridium perfringens
3.4.24.3 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
3.4.24.3 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
3.4.24.3 physiological function the collagenase A produced by Clostridium perfringens seems to be involved in tissue necrosis Clostridium perfringens