Collagenase (non-MMP): Difference between revisions
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'''Collagenase''' (Col) catalyzes the breaking of peptide bonds in collagen. Col cleaves pro-collagen to create collagen. Some collagenases are part of the [[Matrix metalloproteinase]] family. | '''Collagenase''' (Col) catalyzes the breaking of peptide bonds in collagen. Col cleaves pro-collagen to create collagen. Some collagenases are part of the [[Matrix metalloproteinase]] family. | ||
*Collagenase G recognises and unravels collagen microfibrils into triple helices and unwind them<ref>PMID:21947205</ref>. | *'''Collagenase G''' recognises and unravels collagen microfibrils into triple helices and unwind them<ref>PMID:21947205</ref>. | ||
*'''Collagenase H''' targets collagen III<ref>PMID:23768818</ref>. | |||
== Relevance == | == Relevance == |
Latest revision as of 11:41, 5 June 2024
Collagenase (Col) catalyzes the breaking of peptide bonds in collagen. Col cleaves pro-collagen to create collagen. Some collagenases are part of the Matrix metalloproteinase family.
RelevanceCol is used for therapy of wounds, Dupuytren's contracture and Peyronie's disease. Structural highlightsClostridium histolycum collagenase contains several domains among them: peptidase domain (residues 331-721), polycystic kidney disease domain (PKD residues 792-880), collagen-binding domain (CBD residues 1003-1118). The peptidase domain contains a , a and an .[3] Water molecules are shown as red spheres. .
3D Structures of collagenase
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ReferencesReferences
- ↑ Eckhard U, Schonauer E, Nuss D, Brandstetter H. Structure of collagenase G reveals a chew-and-digest mechanism of bacterial collagenolysis. Nat Struct Mol Biol. 2011 Sep 25;18(10):1109-14. doi: 10.1038/nsmb.2127. PMID:21947205 doi:10.1038/nsmb.2127
- ↑ Fujio A, Murayama K, Yamagata Y, Watanabe K, Imura T, Inagaki A, Ohbayashi N, Shima H, Sekiguchi S, Fujimori K, Igarashi K, Ohuchi N, Satomi S, Goto M. Collagenase H is crucial for isolation of rat pancreatic islets. Cell Transplant. 2014;23(10):1187-98. PMID:23768818 doi:10.3727/096368913X668654
- ↑ Eckhard U, Schonauer E, Brandstetter H. Structural basis for activity regulation and substrate preference of clostridial collagenases G, H, and T. J Biol Chem. 2013 May 23. PMID:23703618 doi:10.1074/jbc.M112.448548