Collagenase

Matrix metallopeptidase 1 (interstitial collagenase)
Identifiers
SymbolMMP1
NCBI gene4312
HGNC7155
OMIM120353
RefSeqNM_002421
UniProtP03956
Other data
EC number3.4.24.7
LocusChr. 11 q21-q22
Search for
StructuresSwiss-model
DomainsInterPro
Matrix metallopeptidase 8 (neutrophil collagenase)
Identifiers
SymbolMMP8
NCBI gene4317
HGNC7175
OMIM120355
RefSeqNM_002424
UniProtP22894
Other data
EC numberChromosome = 11 3.4.24.3 Chromosome = 11
Search for
StructuresSwiss-model
DomainsInterPro
Peptidase M9
Identifiers
SymbolPeptidase M9
PfamPF01752
Pfam clanCL0126
InterProIPR013510
MEROPSM9
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Collagenases are enzymes that break the peptide bonds in collagen. They assist in destroying extracellular structures in the pathogenesis of bacteria such as Clostridium. They are considered a virulence factor, facilitating the spread of gas gangrene. They normally target the connective tissue in muscle cells and other body organs.[1]

Collagen, a key component of the animal extracellular matrix, is made through cleavage of pro-collagen by collagenase once it has been secreted from the cell. This stops large structures from forming inside the cell itself.

In addition to being produced by some bacteria, collagenase can be made by the body as part of its normal immune response. This production is induced by cytokines, which stimulate cells such as fibroblasts and osteoblasts, and can cause indirect tissue damage.[citation needed]

  1. ^ Gerard J. Tortora, Berdell R. Funke, Cristine L. Case (2007). Microbiology: an introduction. Pearson Benjamin Cummings. ISBN 978-0-321-39603-7.