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''' (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.
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*Collagenase G recognises and unravels collagen microfibrils into triple helices and unwind them<ref>PMID:21947205</ref>.
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*'''Collagenase G''' recognises and unravels collagen microfibrils into triple helices and unwind them<ref>PMID:21947205</ref>.
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*'''Collagenase H''' targets collagen III<ref>PMID:23768818</ref>.
== Relevance ==
== Relevance ==

Current revision

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

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References

  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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