Biology: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 | ||||||||
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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][excessive citations] 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
- ↑ 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 (8): 1771–1781. doi:10.1271/bbb1961.37.1771.
- ↑ "Purification and characterization of a marine bacterial collagenase". Biochemistry 17 (14): 2857–63. July 1978. doi:10.1021/bi00607a025. PMID 210785.
- ↑ "Circular dichroism comparative studies of two bacterial collagenases and thermolysin". Biochimica et Biophysica Acta (BBA) - Protein Structure 624 (1): 51–9. July 1980. doi:10.1016/0005-2795(80)90224-x. PMID 6250633.
- ↑ "[Purification and study of some properties of a collagenase produced by Empedobacter collagenolyticum]". Biochimie 64 (1): 49–53. January 1982. doi:10.1016/s0300-9084(82)80609-3. PMID 6279175.
- ↑ "Characterization of the individual collagenases from Clostridium histolyticum". Biochemistry 23 (13): 3085–91. June 1984. doi:10.1021/bi00308a036. PMID 6087888.
- ↑ "Relationship between the individual collagenases of Clostridium histolyticum: evidence for evolution by gene duplication". Biochemistry 23 (13): 3092–9. June 1984. doi:10.1021/bi00308a037. PMID 6087889.
- ↑ "Complementary substrate specificities of class I and class II collagenases from Clostridium histolyticum". Biochemistry 24 (23): 6520–6. November 1985. doi:10.1021/bi00344a032. PMID 3002445.
- ↑ Tong, N.T.; Tsugita, A.; Keil-Dlouha, V. (1986). "Purification and characterization of two high-molecular-mass forms of Achromobacter collagenase". Biochim. Biophys. Acta 874 (3): 296–304. doi:10.1016/0167-4838(86)90028-2.
- ↑ "Purification and properties of collagenase from a Streptomyces species". Journal of Biochemistry 102 (1): 163–70. July 1987. doi:10.1093/oxfordjournals.jbchem.a122028. PMID 2822678.
- ↑ "Purification and properties of an extracellular collagenolytic protease produced by the human oral bacterium Bacillus cereus (strain Soc 67)". The Journal of Biological Chemistry 262 (26): 12488–95. September 1987. doi:10.1016/S0021-9258(18)45232-5. PMID 3040751.
External links
- Microbial+collagenase at the US National Library of Medicine Medical Subject Headings (MeSH)
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