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Collagenases are that break the in . They assist in destroying extracellular structures in the pathogenesis of bacteria such as . They are considered a , facilitating the spread of . They normally target the connective tissue in and other body organs.

(2025). 9780321396037, Pearson Benjamin Cummings.

Collagen, a key component of the animal extracellular matrix, is made through 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 , which stimulate cells such as and , and can cause indirect tissue damage.


Therapeutic uses
Collagenases have been approved for medical uses for:


The MEROPS M9 family
This group of metallopeptidases constitutes the peptidase family M9, subfamilies M9A and M9B (microbial collagenase, clan MA(E)). The of the peptidase domain for members of this family resembles that of thermolysin, the type example for clan MA and the predicted residues for members of this family and thermolysin occur in the motif HEXXH.
(1995). 9780121821494

collagenases have been identified from bacteria of both the Vibrio and Clostridium genera. Collagenase is used during bacterial attack to degrade the barrier of the host during invasion. bacteria are sometimes used in hospitals to remove dead tissue from burns and . Clostridium histolyticum is a that causes gas gangrene; nevertheless, the isolated collagenase has been used to treat . Collagen occurs at an in Vibrio bacteria and at bonds in Clostridium collagenases.

Analysis of the primary structure of the product from Clostridium perfringens has revealed that the is produced with a stretch of 86 residues that contain a putative . Within this stretch is found PLGP, an amino acid sequence typical of collagenase substrates. This sequence may thus be implicated in self-processing of the collagenase.

Metalloproteases are the most diverse of the seven main types of , with more than 50 families identified to date. In these enzymes, a cation, usually zinc, activates the water molecule. The metal is held in place by amino acid ligands, usually three in number. The known metal are His, Glu, Asp, or Lys and at least one other residue is required for catalysis, which may play an electrophillic role. Of the known metalloproteases, around half contain an HEXXH motif, which has been shown in crystallographic studies to form part of the metal-binding site. The HEXXH is relatively common, but can be more stringently defined for metalloproteases as 'abXHEbbHbc', where 'a' is most often or threonine and forms part of the S1' subsite in thermolysin and neprilysin, 'b' is an uncharged residue, and 'c' a residue. is never found in this site, possibly because it would break the helical structure adopted by this in metalloproteases.


Other uses
Collagenases may be used for tenderizing meat in a manner similar to widely used tenderizers , and .


See also


External links
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