Collagenase

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Chr. 11 q21-q22
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StructuresSwiss-model
DomainsInterPro
UniProt
P22894
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

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

osteoblasts, and can cause indirect tissue damage.[citation needed
]

Therapeutic uses

Collagenases have been approved for medical uses for:

The MEROPS M9 family

This group of metallopeptidases constitutes the MEROPS peptidase family M9, subfamilies M9A and M9B (microbial collagenase, clan MA(E)). The protein fold of the peptidase domain for members of this family resembles that of thermolysin, the type example for clan MA and the predicted active site residues for members of this family and thermolysin occur in the motif HEXXH.[3]

bed sores. Collagen cleavage occurs at an Xaa+Got in Vibrio bacteria and at Yaa+Gly bonds in Clostridium collagenases.[citation needed
]

Analysis of the

substrates. This sequence may thus be implicated in self-processing of the collagenase.[4]

structure adopted by this motif in metalloproteases.[3]

Other uses

Collagenases may be used for tenderizing meat in a manner similar to widely used tenderizers papain, bromelain and ficain.[5]

See also

References

This article incorporates text from the public domain Pfam and InterPro: IPR013510

External links