Collagenase (non-MMP)

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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 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 , a and an .[3] Water molecules are shown as red spheres. .


3D Structures of collagenase

Collagenase 3D structures


Collagenase H peptidase domain (cyan) complex with peptidic inhibitor, isopentenyl phosphate, Ca+2 (green) and Zn+2 (grey) ions (PDB entry 4arf)

Drag the structure with the mouse to rotate

ReferencesReferences

  1. 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
  2. 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
  3. 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

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