EC 3.4.24.3 - Microbial collagenase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 3.4.24.3

Names

Accepted name:
microbial collagenase
Other names:
Achromobacter iophagus collagenase
Clostridium histolyticum collagenase
Clostridium histolyticum proteinase A
MMP-1
MMP-8
aspergillopeptidase C
azocollase
clostridiopeptidase A
clostridiopeptidase I
clostridiopeptidase II
collagen peptidase
collagen protease
collagenase
collagenase A
collagenase I
collagenase MMP-1
interstitial collagenase
kollaza
matirx metalloproteinase-18
matrix metalloproteinase-1
matrix metalloproteinase-8
metallocollagenase
metalloproteinase-1
nucleolysin
soycollagestin
Systematic name:
-

Reaction

Cofactor

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 [10], Empedobacter collagenolyticum [4], Pseudomonas marinoglutinosa [1], and species of Vibrio, Vibrio B-30 (ATCC 21250) [2] and V. alginolyticus (previously Achromobacter iophagus) [3,8]. Also known from Streptomyces sp. [9]. The Vibrio enzyme is the type example of peptidase family M9. Formerly EC 3.4.99.5, EC 3.4.4.19 and EC 3.4.24.8.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , MEROPS , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004252
CAS Registry Number: 9001-12-1
UniProtKB/Swiss-Prot:

References

  1. Hanada, K., Mizutani, T., Yamagishi, M., Tsuji, H., Misaki, T. Sawada, J.
    The isolation of collagenase and its enzymological and physico-chemical properties.
    Agric. Biol. Chem. 37 : 1771-1781 (1973).
  2. Merkel, J.R. and Dreisbach, J.H.
    Purification and characterization of a marine bacterial collagenase.
    Biochemistry 17 : 2857-2863 (1978). [PMID: 210785]
  3. Heindl, M.-C., Fermandjian, S. and Keil, B.
    Circular dichroism comparative studies of two bacterial collagenases and thermolysin.
    Biochim. Biophys. Acta 624 : 51-59 (1980). [PMID: 6250633]
  4. Labadie, J. and Montel, M..-C.
    Purification et étude de quelques propriétés d'une collagénase produite par Empedobacter collagenolyticum.
    Biochimie 64 : 49-54 (1982). [PMID: 6530724]
  5. Bond, M.D and Van Wart, H.D.
    Characterization of the individual collagenases from Clostridium histolyticum.
    Biochemistry 23 : 3085-3091 (1984). [PMID: 6087888]
  6. Bond, M.D. and Van Wart, H.D.
    Relationship between the individual collagenases of Clostridium histolyticum: evidience for evolution by gene duplication.
    Biochemistry 23 : 3092-3099 (1984). [PMID: 6087889]
  7. Van Wart, H.D. and Steinbrink, D.R.
    Complementary substrate specificities of class I and class II collagenases from Clostridium histolyticum.
    Biochemistry 24 : 6520-6526 (1985). [PMID: 3002445]
  8. Tong, N.T., Tsugita, A. and Keil-Dlouha, V.
    Purification and characterization of two high-molecular-mass forms of Achromobacter collagenase.
    Biochim. Biophys. Acta. 874 : 296-304 (1986).
  9. Endo, A., Murakawa, S., Shimizu, H. and Shiraishi, Y.
    Purification and properties of collagenase from a Streptomyces species.
    J. Biochem. (Tokyo) 102 : 163-170 (1987). [PMID: 2822678]
  10. Makinen, K.K. and Makinen, P.-L.
    Purification and properties of an extracellular collagenolytic protease produced by the human oral bacterium Bacillus cereus (strain Soc 67).
    J. Biol. Chem. 262 : 12488-12495 (1987). [PMID: 3040751]

[EC 3.4.24.3 created 1961 as EC 3.4.4.19, transferred 1972 to EC 3.4.24.3 (EC 3.4.24.8 created 1978, incorporated 1992, EC 3.4.99.5 created 1972, incorporated 1978)]