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Information on EC 3.4.24.3 - microbial collagenase

for references in articles please use BRENDA:EC3.4.24.3

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IUBMB Comments

Six species of metalloendopeptidase acting on native collagen can be isolated from the medium of Clostridium histolyticum. Class I has forms α (68 kDa), β (115 kDa) and γ (79 kDa); class II has δ (100 kDa), ε (110 kDa) and ζ (125 kDa). The two classes are immunologically crossreactive, but have significantly different sequences, and different specificities such that their actions on collagen are complementary. The enzymes also act as peptidyl-tripeptidases. Variants of the enzyme have been purified from Bacillus cereus , Empedobacter collagenolyticum , Pseudomonas marinoglutinosa , and species of Vibrio, Vibrio B-30 (ATCC 21250) and V. alginolyticus (previously Achromobacter iophagus) [3,8]. Also known from Streptomyces sp. . The Vibrio enzyme is the type example of peptidase family M9.

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

REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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'
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