Microbial collagenase

Microbial collagenase
Identifiers
EC number 3.4.24.3
CAS number 2593923
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Microbial collagenase (EC 3.4.24.3, Clostridium histolyticum collagenase, clostridiopeptidase A, collagenase A, collagenase I, Achromobacter iophagus collagenase, collagenase, aspergillopeptidase C, nucleolysin, azocollase, metallocollagenase, soycollagestin, Clostridium histolyticum proteinase A, clostridiopeptidase II, MMP-8, clostridiopeptidase I, collagen peptidase, collagen protease, collagenase MMP-1, metalloproteinase-1, kollaza, matrix metalloproteinase-1, matrix metalloproteinase-8, matirx metalloproteinase-18, interstitial collagenase) is an enzyme.[1][2][3][4][5][6][7][8][9][10] This enzyme catalyses the following chemical reaction

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'

Six species of metalloendopeptidase acting on native collagen can be isolated from the medium of Clostridium histolyticum.

See also

References

  1. ↑ Hanada, K., Mizutani, T., Yamagishi, M., Tsuji, H., Misaki, T. Sawada, J. (1973). "The isolation of collagenase and its enzymological and physico-chemical properties". Agric. Biol. Chem. 37: 1771–1781. doi:10.1271/bbb1961.37.1771.
  2. ↑ Merkel, J.R. and Dreisbach, J.H. (1978). "Purification and characterization of a marine bacterial collagenase". Biochemistry 17: 2857–2863. doi:10.1021/bi00607a025. PMID 210785.
  3. ↑ Heindl, M.-C., Fermandjian, S. and Keil, B. (1980). "Circular dichroism comparative studies of two bacterial collagenases and thermolysin". Biochim. Biophys. Acta 624: 51–59. doi:10.1016/0005-2795(80)90224-x. PMID 6250633.
  4. ↑ Labadie, J. and Montel, M..-C. (1982). "Purification et étude de quelques propriétés d’une collagénase produite par Empedobacter collagenolyticum". Biochimie 64: 49–54. doi:10.1016/s0300-9084(82)80609-3. PMID 6530724.
  5. ↑ Bond, M.D and Van Wart, H.D. (1984). "Characterization of the individual collagenases from Clostridium histolyticum". Biochemistry 23: 3085–3091. doi:10.1021/bi00308a036. PMID 6087888.
  6. ↑ Bond, M.D. and Van Wart, H.D. (1984). "Relationship between the individual collagenases of Clostridium histolyticum: evidence for evolution by gene duplication". Biochemistry 23: 3092–3099. doi:10.1021/bi00308a037. PMID 6087889.
  7. ↑ Van Wart, H.D. and Steinbrink, D.R. (1985). "Complementary substrate specificities of class I and class II collagenases from Clostridium histolyticum". Biochemistry 24: 6520–6526. doi:10.1021/bi00344a032. PMID 3002445.
  8. ↑ Tong, N.T., Tsugita, A. and Keil-Dlouha, V. (1986). "Purification and characterization of two high-molecular-mass forms of Achromobacter collagenase". Biochim. Biophys. Acta 874: 296–304. doi:10.1016/0167-4838(86)90028-2.
  9. ↑ Endo, A., Murakawa, S., Shimizu, H. and Shiraishi, Y. (1987). "Purification and properties of collagenase from a Streptomyces species". J. Biochem. (Tokyo) 102: 163–170. PMID 2822678.
  10. ↑ Makinen, K.K. and Makinen, P.-L. (1987). "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. PMID 3040751.

External links

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