Collagenase: Difference between revisions
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{{protein | Name = [[MMP1| | {{infobox protein | ||
{{protein | Name = | | Name = [[MMP1|Matrix metallopeptidase 1 (interstitial collagenase)]] | ||
'''Collagenases''' are [[enzymes]] that break the [[peptide bonds]] in [[collagen]]. | | caption = | ||
| image = | |||
| width = | |||
| HGNCid = 7155 | |||
| Symbol = [[MMP1]] | |||
| AltSymbols = | |||
| EntrezGene = 4312 | |||
| OMIM = 120353 | |||
| RefSeq = NM_002421 | |||
| UniProt = P03956 | |||
| PDB = | |||
| ECnumber = 3.4.24.7 | |||
| Chromosome = 11 | |||
| Arm = q | |||
| Band = 21 | |||
| LocusSupplementaryData = -q22 | |||
}} | |||
{{infobox protein | |||
| Name = [[MMP8|Matrix metallopeptidase 8 (neutrophil collagenase)]] | |||
| caption = | |||
| image = | |||
| width = | |||
| HGNCid = 7175 | |||
| Symbol = [[MMP8]] | |||
| AltSymbols = | |||
| EntrezGene = 4317 | |||
| OMIM = 120355 | |||
| RefSeq = NM_002424 | |||
| UniProt = P22894 | |||
| PDB = | |||
| ECnumber = 3.4.24.3 Chromosome = 11 | |||
| Arm = q | |||
| Band = 21 | |||
| LocusSupplementaryData = -q22 | |||
}} | |||
{{Infobox protein family | |||
| Name = Peptidase M9 | |||
| Symbol = Peptidase M9 | |||
| image = | |||
| width = | |||
| caption = | |||
| Pfam = PF01752 | |||
| Pfam_clan = CL0126 | |||
| InterPro = IPR013510 | |||
| SMART = | |||
| PROSITE = | |||
| MEROPS = M9 | |||
| SCOP = | |||
| TCDB = | |||
| OPM family = | |||
| OPM protein = | |||
| CAZy = | |||
| CDD = | |||
}} | |||
'''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.<ref>{{cite book |author=Gerard J. Tortora |author2=Berdell R. Funke |author3=Cristine L. Case |title=Microbiology: an introduction |publisher=Pearson Benjamin Cummings |year=2007 |isbn=0-321-39603-0}}</ref> | |||
Collagen, a key component of the animal extracellular matrix, is made through [[Bond cleavage|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 [[cytokine]]s, which stimulate cells such as [[fibroblasts]] and [[osteoblasts]], and can cause indirect tissue damage.{{Citation needed|date=November 2007}} | |||
==Therapeutic uses== | |||
Collagenases have been approved for medical uses for | |||
* treatment of [[Dupuytren's contracture]] and [[Peyronie's disease]] ([[Xiaflex]]). | |||
* [[wound healing]]<ref>{{cite journal | pmc = 1501117 | pmid=16921413 | volume=4 | title=Collagenase promotes the cellular responses to injury and wound healing in vivo | year=2005 | journal=J Burns Wounds | pages=e8 | vauthors=Riley KN, Herman IM}}</ref> (Santyl) | |||
===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 folding|protein fold]] of the peptidase [[Domain (biology)|domain]] for members of this family resembles that of thermolysin, the type example for clan MA and the predicted [[active site]] [[Residue (chemistry)|residue]]s for members of this family and thermolysin occur in the motif HEXXH.<ref name="pmid7674922">{{cite journal | vauthors = Rawlings ND, Barrett AJ | title = Evolutionary families of metallopeptidases | journal = Meth. Enzymol. | volume = 248 | issue = | pages = 183–228 | year = 1995 | pmid = 7674922 | doi = 10.1016/0076-6879(95)48015-3| url = }}</ref> | |||
[[microbe|Microbial]] collagenases have been identified from [[Zinc dependent phospholipase C|bacteria]] of both the ''Vibrio'' and ''Clostridium'' genera. Collagenase is used during bacterial attack to degrade the [[collagen]] barrier of the host during invasion. ''[[Vibrio]]'' bacteria are sometimes used in hospitals to remove dead [[tissue (biology)|tissue]] from burns and [[peptic ulcer|ulcers]]. ''Clostridium histolyticum'' is a [[pathogen]] that causes gas gangrene; nevertheless, the isolated collagenase has been used to treat [[bed sores]]. Collagen [[Bond cleavage|cleavage]] occurs at an {{no wrap|Xaa+Got}} in ''Vibrio'' bacteria and at {{no wrap|Yaa+Gly}} bonds in ''Clostridium'' collagenases. | |||
Analysis of the [[primary structure]] of the [[gene]] [[product (chemistry)|product]] from ''Clostridium perfringens'' has revealed that the [[enzyme]] is produced with a stretch of 86 [[Residue (chemistry)|residues]] that contain a putative [[Signal peptide|signal sequence]].<ref name="pmid8282691">{{cite journal | vauthors = Matsushita O, Yoshihara K, Katayama S, Minami J, Okabe A | title = Purification and characterization of Clostridium perfringens 120-kilodalton collagenase and nucleotide sequence of the corresponding gene | journal = J. Bacteriol. | volume = 176 | issue = 1 | pages = 149–56 |date=January 1994 | pmid = 8282691 | pmc = 205026 | doi = | url = }}</ref> Within this stretch is found PLGP, an [[amino acid sequence]] typical of collagenase [[substrate (biochemistry)|substrates]]. This [[sequence (biology)|sequence]] may thus be implicated in self-processing of the collagenase.<ref name="pmid8282691"/> | |||
[[Metalloproteinase|Metalloproteases]] are the most diverse of the seven main types of [[protease]], with more than 50 families identified to date. In these enzymes, a [[divalent]] cation, usually zinc, activates the water molecule. The metal [[ion]] is held in place by [[Amino acid#Chemical properties|amino acid]] ligands, usually three in number. The known metal [[ligands]] are His, Glu, Asp, or Lys and at least one other [[Residue (chemistry)|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.<ref name="pmid7674922"/> The HEXXH [[protein motif|motif]] is relatively common, but can be more stringently defined for metalloproteases as 'abXHEbbHbc', where 'a' is most often [[valine]] or threonine and forms part of the S1' subsite in thermolysin and neprilysin, 'b' is an uncharged residue, and 'c' a [[hydrophobic]] [[Residue (chemistry)|residue]]. [[Proline]] is never found in this site, possibly because it would break the helical [[secondary structure|structure]] adopted by this [[sequence motif|motif]] in metalloproteases.<ref name="pmid7674922"/> | |||
== Other uses == | |||
Collagenases may be used for tenderizing meat in a manner similar to widely used tenderizers [[papain]], [[bromelain]] and [[ficain]].<ref>{{Cite journal|last=Zhao|first=Guo-Yan|last2=Zhou|first2=Ming-Yang|last3=Zhao|first3=Hui-Lin|last4=Chen|first4=Xiu-Lan|last5=Xie|first5=Bin-Bin|last6=Zhang|first6=Xi-Ying|last7=He|first7=Hai-Lun|last8=Zhou|first8=Bai-Cheng|last9=Zhang|first9=Yu-Zhong|date=2012-10-15|title=Tenderization effect of cold-adapted collagenolytic protease MCP-01 on beef meat at low temperature and its mechanism|url=https://www.ncbi.nlm.nih.gov/pubmed/23442615|journal=Food Chemistry|volume=134|issue=4|pages=1738–1744|doi=10.1016/j.foodchem.2012.03.118|issn=0308-8146|pmid=23442615}}</ref> | |||
==See also== | ==See also== | ||
| Line 16: | Line 84: | ||
==References== | ==References== | ||
{{ | {{InterPro content|IPR013510}} | ||
{{Reflist|2}} | |||
==External links== | ==External links== | ||
* {{MeshName|Collagenases}} | * {{MeshName|Collagenases}} | ||
{{ | {{Metalloendopeptidases}} | ||
{{ | {{Enzymes}} | ||
{{Portal bar|Molecular and Cellular Biology|border=no}} | |||
[[Category:EC 3.4.24]] | [[Category:EC 3.4.24]] | ||
[[Category:Protein families]] | |||
[[ | |||
Revision as of 16:34, 29 November 2017
| Matrix metallopeptidase 1 (interstitial collagenase) | |
|---|---|
| Identifiers | |
| Symbol | MMP1 |
| Entrez | 4312 |
| HUGO | 7155 |
| OMIM | 120353 |
| RefSeq | NM_002421 |
| UniProt | P03956 |
| Other data | |
| EC number | 3.4.24.7 |
| Locus | Chr. 11 q21-q22 |
| Matrix metallopeptidase 8 (neutrophil collagenase) | |
|---|---|
| Identifiers | |
| Symbol | MMP8 |
| Entrez | 4317 |
| HUGO | 7175 |
| OMIM | 120355 |
| RefSeq | NM_002424 |
| UniProt | P22894 |
| Other data | |
| EC number | Chromosome = 11 3.4.24.3 Chromosome = 11 |
| Peptidase M9 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Peptidase M9 | ||||||||
| Pfam | PF01752 | ||||||||
| Pfam clan | CL0126 | ||||||||
| InterPro | IPR013510 | ||||||||
| MEROPS | M9 | ||||||||
| |||||||||
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]
Therapeutic uses
Collagenases have been approved for medical uses for
- treatment of Dupuytren's contracture and Peyronie's disease (Xiaflex).
- wound healing[2] (Santyl)
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]
Microbial collagenases have been identified from bacteria of both the Vibrio and Clostridium genera. Collagenase is used during bacterial attack to degrade the collagen barrier of the host during invasion. Vibrio bacteria are sometimes used in hospitals to remove dead tissue from burns and ulcers. Clostridium histolyticum is a pathogen that causes gas gangrene; nevertheless, the isolated collagenase has been used to treat bed sores. Collagen cleavage occurs at an Xaa+Got in Vibrio bacteria and at Yaa+Gly bonds in Clostridium collagenases.
Analysis of the primary structure of the gene product from Clostridium perfringens has revealed that the enzyme is produced with a stretch of 86 residues that contain a putative signal sequence.[4] 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.[4]
Metalloproteases are the most diverse of the seven main types of protease, with more than 50 families identified to date. In these enzymes, a divalent cation, usually zinc, activates the water molecule. The metal ion is held in place by amino acid ligands, usually three in number. The known metal ligands 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.[3] The HEXXH motif is relatively common, but can be more stringently defined for metalloproteases as 'abXHEbbHbc', where 'a' is most often valine or threonine and forms part of the S1' subsite in thermolysin and neprilysin, 'b' is an uncharged residue, and 'c' a hydrophobic residue. Proline is never found in this site, possibly because it would break the helical 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
- ↑ Gerard J. Tortora; Berdell R. Funke; Cristine L. Case (2007). Microbiology: an introduction. Pearson Benjamin Cummings. ISBN 0-321-39603-0.
- ↑ Riley KN, Herman IM (2005). "Collagenase promotes the cellular responses to injury and wound healing in vivo". J Burns Wounds. 4: e8. PMC 1501117. PMID 16921413.
- ↑ 3.0 3.1 3.2 Rawlings ND, Barrett AJ (1995). "Evolutionary families of metallopeptidases". Meth. Enzymol. 248: 183–228. doi:10.1016/0076-6879(95)48015-3. PMID 7674922.
- ↑ 4.0 4.1 Matsushita O, Yoshihara K, Katayama S, Minami J, Okabe A (January 1994). "Purification and characterization of Clostridium perfringens 120-kilodalton collagenase and nucleotide sequence of the corresponding gene". J. Bacteriol. 176 (1): 149–56. PMC 205026. PMID 8282691.
- ↑ Zhao, Guo-Yan; Zhou, Ming-Yang; Zhao, Hui-Lin; Chen, Xiu-Lan; Xie, Bin-Bin; Zhang, Xi-Ying; He, Hai-Lun; Zhou, Bai-Cheng; Zhang, Yu-Zhong (2012-10-15). "Tenderization effect of cold-adapted collagenolytic protease MCP-01 on beef meat at low temperature and its mechanism". Food Chemistry. 134 (4): 1738–1744. doi:10.1016/j.foodchem.2012.03.118. ISSN 0308-8146. PMID 23442615.
External links
- Collagenases at the US National Library of Medicine Medical Subject Headings (MeSH)