:Microbial collagenase

{{Infobox enzyme

| Name = Microbial collagenase

| EC_number = 3.4.24.3

| CAS_number = 2593923

| GO_code =

| image =

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Microbial collagenase ({{EC number|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.{{cite journal | title = The isolation of collagenase and its enzymological and physico-chemical properties |author1 = Hanada, K. |author2 = Mizutani, T. |author3 = Yamagishi, M. |author4 = Tsuji, H. |author5 = Misaki, T. |author6 = Sawada, J. |journal = Agric. Biol. Chem. |date = 1973 |volume = 37 |issue = 8 |pages = 1771–1781 |doi=10.1271/bbb1961.37.1771|doi-access = }}{{cite journal | vauthors = Merkel JR, Dreisbach JH | title = Purification and characterization of a marine bacterial collagenase | journal = Biochemistry | volume = 17 | issue = 14 | pages = 2857–63 | date = July 1978 | pmid = 210785 | doi = 10.1021/bi00607a025 }}{{cite journal | vauthors = Heindl MC, Fermandjian S, Keil B | title = Circular dichroism comparative studies of two bacterial collagenases and thermolysin | journal = Biochimica et Biophysica Acta (BBA) - Protein Structure | volume = 624 | issue = 1 | pages = 51–9 | date = July 1980 | pmid = 6250633 | doi = 10.1016/0005-2795(80)90224-x }}{{cite journal | vauthors = Labadie J, Montel MC | title = [Purification and study of some properties of a collagenase produced by Empedobacter collagenolyticum] | journal = Biochimie | volume = 64 | issue = 1 | pages = 49–53 | date = January 1982 | pmid = 6279175 | doi = 10.1016/s0300-9084(82)80609-3 }}{{cite journal | vauthors = Bond MD, Van Wart HE | title = Characterization of the individual collagenases from Clostridium histolyticum | journal = Biochemistry | volume = 23 | issue = 13 | pages = 3085–91 | date = June 1984 | pmid = 6087888 | doi = 10.1021/bi00308a036 }}{{cite journal | vauthors = Bond MD, Van Wart HE | title = Relationship between the individual collagenases of Clostridium histolyticum: evidence for evolution by gene duplication | journal = Biochemistry | volume = 23 | issue = 13 | pages = 3092–9 | date = June 1984 | pmid = 6087889 | doi = 10.1021/bi00308a037 }}{{cite journal | vauthors = Van Wart HE, Steinbrink DR | title = Complementary substrate specificities of class I and class II collagenases from Clostridium histolyticum | journal = Biochemistry | volume = 24 | issue = 23 | pages = 6520–6 | date = November 1985 | pmid = 3002445 | doi = 10.1021/bi00344a032 }}{{cite journal | title = Purification and characterization of two high-molecular-mass forms of Achromobacter collagenase |author = Tong, N.T. |author2 = Tsugita, A. |author3 = Keil-Dlouha, V. |journal = Biochim. Biophys. Acta |date = 1986 |volume = 874 |issue = 3 |pages = 296–304 |doi=10.1016/0167-4838(86)90028-2}}{{cite journal | vauthors = Endo A, Murakawa S, Shimizu H, Shiraishi Y | title = Purification and properties of collagenase from a Streptomyces species | journal = Journal of Biochemistry | volume = 102 | issue = 1 | pages = 163–70 | date = July 1987 | pmid = 2822678 | doi = 10.1093/oxfordjournals.jbchem.a122028 }}{{cite journal | vauthors = Makinen KK, Makinen PL | title = Purification and properties of an extracellular collagenolytic protease produced by the human oral bacterium Bacillus cereus (strain Soc 67) | journal = The Journal of Biological Chemistry | volume = 262 | issue = 26 | pages = 12488–95 | date = September 1987 | doi = 10.1016/S0021-9258(18)45232-5 | pmid = 3040751 | doi-access = free }}{{Excessive citations inline|date=August 2021}} 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.