Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.4.24.3 - microbial collagenase and Organism(s) Vibrio cholerae serotype O1 and UniProt Accession Q9KRJ0

for references in articles please use BRENDA:EC3.4.24.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.3 microbial collagenase
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Vibrio cholerae serotype O1
UNIPROT: Q9KRJ0 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
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
bacterial collagenase, collagenase clostridium histolyticum, type i collagenase, collagenase i, clostridial collagenase, clostridium histolyticum collagenase, type ii collagenase, clostridiopeptidase a, collagenase g, collagenase h, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
bacterial collagenase
-
class II collagenase
-
microbial collagenase
-
120 kDa collagenase
-
-
-
-
Achromobacter iophagus collagenase
-
-
-
-
aspergillopeptidase C
-
-
-
-
azocollase
-
-
-
-
clostridiopeptidase A
-
-
-
-
clostridiopeptidase I
-
-
-
-
clostridiopeptidase II
-
-
-
-
Clostridium histolyticum collagenase
-
-
-
-
collagen peptidase
-
-
-
-
collagen protease
-
-
-
-
collagenase A
-
-
-
-
collagenase I
-
-
-
-
collagenase MMP-1
-
-
-
-
kollaza
-
-
-
-
matirx metalloproteinase-18
-
-
-
-
matrix metalloproteinase-1
-
-
-
-
metallocollagenase
-
-
-
-
metalloproteinase-1
-
-
-
-
MMP-1
-
-
-
-
nucleolysin
-
-
-
-
peptidase, clostridio-, A
-
-
-
-
proteinase, Clostridium histolyticum, A
-
-
-
-
soycollagestin
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9001-12-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Collagen + H2O
?
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Collagen + H2O
?
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
a zinc metalloproteinase
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Duarte, A.; Correia, A.; Esteves, A.
Bacterial collagenases - a review
Crit. Rev. Microbiol.
42
106-126
2016
Vibrio mimicus (O67990), Clostridium perfringens (P43153), Vibrio alginolyticus (P43154), Hathewaya histolytica (Q46085), Hathewaya histolytica (Q9X721), Bacillus cereus (Q4V1V2), Bacillus cereus (Q81DA6), Vibrio parahaemolyticus RIMD 2210633 (Q56696), Vibrio parahaemolyticus (Q9AMB9), Vibrio cholerae serotype O1 (Q9KRJ0), Bacillus cereus ATCC 14579 (Q81DA6), Bacillus cereus NRRL B-3711 (Q81DA6), Bacillus cereus NCIMB 9373 (Q81DA6), Bacillus cereus DSM 31 (Q81DA6), Clostridium perfringens type A (P43153), Bacillus cereus NBRC 15305 (Q81DA6), Clostridium perfringens 13 (P43153), Bacillus cereus ZK (Q4V1V2), Vibrio cholerae serotype O1 El Tor Inaba N16961 (Q9KRJ0), Bacillus cereus JCM 2152 (Q81DA6), Vibrio parahaemolyticus 04 (Q9AMB9), Bacillus cereus E33L (Q4V1V2), Vibrio cholerae serotype O1 ATCC 39315 (Q9KRJ0)
Manually annotated by BRENDA team