| Identification |
|---|
| HMDB Protein ID
| HMDBP13398 |
| Secondary Accession Numbers
| None |
| Name
| Karilysin |
| Synonyms
|
- Matrix metalloprotease-like enzyme
- MMP-like enzyme
|
| Gene Name
| KLY |
| Protein Type
| Unknown |
| Biological Properties |
|---|
| General Function
| Not Available |
| Specific Function
| Metalloprotease able to cleave casein, gelatin, elastin, fibrinogen and fibronectin. Shows exclusive preference for hydrophobic residues, especially Leu, Tyr and Met, at the P1' position of substrates, and for Pro or Ala at P3. Can efficiently cleave the antimicrobial peptide LL-37 which is a component of the immune system, leading to a significant reduction of its bactericidal activity. Is also able to inhibit all pathways of the human complement system. The classical and lectin complement pathways are inhibited because of the efficient degradation of mannose-binding lectin, ficolin-2, ficolin-3, and C4 by karilysin, whereas inhibition of the terminal pathway is caused by cleavage of C5. Thus, karilysin appears to be a major virulence factor of T.forsythia that contributes to evasion of the human immune response and periodontal disease. Seems to act synergistically with gingipains from the periodontal pathogen P.gingivalis present at the same sites of infection. |
| Pathways
|
Not Available
|
| Reactions
| Not Available |
| GO Classification
|
| Biological Process |
| pathogenesis |
| Cellular Component |
| extracellular region |
| extracellular matrix |
| Molecular Function |
| metalloendopeptidase activity |
| zinc ion binding |
|
| Cellular Location
|
Not Available
|
| Gene Properties |
|---|
| Chromosome Location
| Not Available |
| Locus
| Not Available |
| SNPs
| Not Available |
| Gene Sequence
|
Not Available
|
| Protein Properties |
|---|
| Number of Residues
| Not Available |
| Molecular Weight
| 52060.205 |
| Theoretical pI
| Not Available |
| Pfam Domain Function
|
|
| Signals
|
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
Not Available
|
| External Links |
|---|
| GenBank ID Protein
| Not Available |
| UniProtKB/Swiss-Prot ID
| D0EM77 |
| UniProtKB/Swiss-Prot Entry Name
| KLY_TANFA |
| PDB IDs
|
|
| GenBank Gene ID
| Not Available |
| GeneCard ID
| Not Available |
| GenAtlas ID
| Not Available |
| HGNC ID
| Not Available |
| References |
|---|
| General References
| - Karim AY, Kulczycka M, Kantyka T, Dubin G, Jabaiah A, Daugherty PS, Thogersen IB, Enghild JJ, Nguyen KA, Potempa J: A novel matrix metalloprotease-like enzyme (karilysin) of the periodontal pathogen Tannerella forsythia ATCC 43037. Biol Chem. 2010 Jan;391(1):105-17. doi: 10.1515/BC.2010.009. [PubMed:19919176 ]
- Koziel J, Karim AY, Przybyszewska K, Ksiazek M, Rapala-Kozik M, Nguyen KA, Potempa J: Proteolytic inactivation of LL-37 by karilysin, a novel virulence mechanism of Tannerella forsythia. J Innate Immun. 2010;2(3):288-93. doi: 10.1159/000281881. Epub 2010 Feb 4. [PubMed:20375548 ]
- Jusko M, Potempa J, Karim AY, Ksiazek M, Riesbeck K, Garred P, Eick S, Blom AM: A metalloproteinase karilysin present in the majority of Tannerella forsythia isolates inhibits all pathways of the complement system. J Immunol. 2012 Mar 1;188(5):2338-49. doi: 10.4049/jimmunol.1101240. Epub 2012 Jan 27. [PubMed:22287711 ]
- Skottrup PD, Sorensen G, Ksiazek M, Potempa J, Riise E: A phage display selected 7-mer peptide inhibitor of the Tannerella forsythia metalloprotease-like enzyme Karilysin can be truncated to Ser-Trp-Phe-Pro. PLoS One. 2012;7(10):e48537. doi: 10.1371/journal.pone.0048537. Epub 2012 Oct 31. [PubMed:23119051 ]
- Cerda-Costa N, Guevara T, Karim AY, Ksiazek M, Nguyen KA, Arolas JL, Potempa J, Gomis-Ruth FX: The structure of the catalytic domain of Tannerella forsythia karilysin reveals it is a bacterial xenologue of animal matrix metalloproteinases. Mol Microbiol. 2011 Jan;79(1):119-32. doi: 10.1111/j.1365-2958.2010.07434.x. Epub 2010 Nov 2. [PubMed:21166898 ]
- Guevara T, Ksiazek M, Skottrup PD, Cerda-Costa N, Trillo-Muyo S, de Diego I, Riise E, Potempa J, Gomis-Ruth FX: Structure of the catalytic domain of the Tannerella forsythia matrix metallopeptidase karilysin in complex with a tetrapeptidic inhibitor. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 May 1;69(Pt 5):472-6. doi: 10.1107/S1744309113007392. Epub 2013 Apr 27. [PubMed:23695557 ]
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