Microbial collagenase
| Microbial collagenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.24.3 | ||||||||
| CAS no. | 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][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.
- ^ Merkel JR, Dreisbach JH (July 1978). "Purification and characterization of a marine bacterial collagenase". Biochemistry. 17 (14): 2857–63. doi:10.1021/bi00607a025. PMID 210785.
- ^ Heindl MC, Fermandjian S, Keil B (July 1980). "Circular dichroism comparative studies of two bacterial collagenases and thermolysin". Biochimica et Biophysica Acta (BBA) - Protein Structure. 624 (1): 51–9. doi:10.1016/0005-2795(80)90224-x. PMID 6250633.
- ^ Labadie J, Montel MC (January 1982). "[Purification and study of some properties of a collagenase produced by Empedobacter collagenolyticum]". Biochimie. 64 (1): 49–53. doi:10.1016/s0300-9084(82)80609-3. PMID 6279175.
- ^ Bond MD, Van Wart HE (June 1984). "Characterization of the individual collagenases from Clostridium histolyticum". Biochemistry. 23 (13): 3085–91. doi:10.1021/bi00308a036. PMID 6087888.
- ^ Bond MD, Van Wart HE (June 1984). "Relationship between the individual collagenases of Clostridium histolyticum: evidence for evolution by gene duplication". Biochemistry. 23 (13): 3092–9. doi:10.1021/bi00308a037. PMID 6087889.
- ^ Van Wart HE, Steinbrink DR (November 1985). "Complementary substrate specificities of class I and class II collagenases from Clostridium histolyticum". Biochemistry. 24 (23): 6520–6. 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.
- ^ Endo A, Murakawa S, Shimizu H, Shiraishi Y (July 1987). "Purification and properties of collagenase from a Streptomyces species". Journal of Biochemistry. 102 (1): 163–70. doi:10.1093/oxfordjournals.jbchem.a122028. PMID 2822678.
- ^ Makinen KK, Makinen PL (September 1987). "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. doi:10.1016/S0021-9258(18)45232-5. PMID 3040751.
External links
- Microbial+collagenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
