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[1].
- Collagenase H targets collagen III[2].
Relevance
Col is used for therapy of wounds, Dupuytren's contracture and Peyronie's disease.
Structural highlights
Clostridium 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 Zn+2 coordination site, a substrate-recognition site and an oxyanion hole.[3] Water molecules are shown as red spheres. Click here to see surface of binding site.
3D Structures of collagenase
Collagenase 3D structures
- ↑ 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
