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A novel matrix metalloprotease-like enzyme (karilysin) of the periodontal pathogen Tannerella forsythia ATCC 43037

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A novel matrix metalloprotease-like enzyme (karilysin) of the periodontal pathogen Tannerella forsythia ATCC 43037. / Karim, Abdulkarim Y; Kulczycka, Magdalena; Kantyka, Tomasz; Dubin, Grzegorz; Jabaiah, Abeer; Daugherty, Patrick S; Thogersen, Ida B; Enghild, Jan J; Nguyen, Ky-Anh; Potempa, Jan.

I: Biological Chemistry, 2009.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Karim, AY, Kulczycka, M, Kantyka, T, Dubin, G, Jabaiah, A, Daugherty, PS, Thogersen, IB, Enghild, JJ, Nguyen, K-A & Potempa, J 2009, 'A novel matrix metalloprotease-like enzyme (karilysin) of the periodontal pathogen Tannerella forsythia ATCC 43037', Biological Chemistry. https://doi.org/10.1515/BC.2010.009

APA

Karim, A. Y., Kulczycka, M., Kantyka, T., Dubin, G., Jabaiah, A., Daugherty, P. S., ... Potempa, J. (2009). A novel matrix metalloprotease-like enzyme (karilysin) of the periodontal pathogen Tannerella forsythia ATCC 43037. Biological Chemistry. https://doi.org/10.1515/BC.2010.009

CBE

Karim AY, Kulczycka M, Kantyka T, Dubin G, Jabaiah A, Daugherty PS, Thogersen IB, Enghild JJ, Nguyen K-A, Potempa J. 2009. A novel matrix metalloprotease-like enzyme (karilysin) of the periodontal pathogen Tannerella forsythia ATCC 43037. Biological Chemistry. https://doi.org/10.1515/BC.2010.009

MLA

Vancouver

Karim AY, Kulczycka M, Kantyka T, Dubin G, Jabaiah A, Daugherty PS o.a. A novel matrix metalloprotease-like enzyme (karilysin) of the periodontal pathogen Tannerella forsythia ATCC 43037. Biological Chemistry. 2009. https://doi.org/10.1515/BC.2010.009

Author

Karim, Abdulkarim Y ; Kulczycka, Magdalena ; Kantyka, Tomasz ; Dubin, Grzegorz ; Jabaiah, Abeer ; Daugherty, Patrick S ; Thogersen, Ida B ; Enghild, Jan J ; Nguyen, Ky-Anh ; Potempa, Jan. / A novel matrix metalloprotease-like enzyme (karilysin) of the periodontal pathogen Tannerella forsythia ATCC 43037. I: Biological Chemistry. 2009.

Bibtex

@article{037103a0fa1c11de9c17000ea68e967b,
title = "A novel matrix metalloprotease-like enzyme (karilysin) of the periodontal pathogen Tannerella forsythia ATCC 43037",
abstract = "Abstract Proteases of Tannerella forsythia, a pathogen associated with periodontal disease, are implicated as virulence factors. Here, we characterized a matrix metalloprotease (MMP)-like enzyme of T. forsythia referred to as karilysin. Full-length (without a signal peptide) recombinant karilysin (49.9 kDa) processed itself into the mature 18 kDa enzyme through sequential autoproteolytic cleavages both at N- and C-terminal profragments. The first cleavage at the Asn14-Tyr15 peptide bond generated the fully active enzyme (47.9 kDa) and subsequent truncations at the C-termini did not affect proteolytic activity. Mutation of Tyr15 to Ala generated a prokarilysin variant that processed itself into the final 18 kDa form with greatly reduced kinetics. Inactive prokarilysin with the mutated catalytic Glu residue (E136A) was processed by active karilysin at the same sites as the active enzymes. The karilysin proteolytic activity and autoprocessing were inhibited by 1,10-phenanthroline and EDTA. Calcium ions were found to be important for both activity and thermal stability of karilysin. Using the CLiPS technology, the specificity of karilysin was found to be similar to that of MMPs with preference for Leu/Tyr/Met at P1' and Pro/Ala at P3. This specificity and the ability to degrade elastin, fibrinogen and fibronectin may contribute to the pathogenicity of periodontitis.",
author = "Karim, {Abdulkarim Y} and Magdalena Kulczycka and Tomasz Kantyka and Grzegorz Dubin and Abeer Jabaiah and Daugherty, {Patrick S} and Thogersen, {Ida B} and Enghild, {Jan J} and Ky-Anh Nguyen and Jan Potempa",
year = "2009",
doi = "10.1515/BC.2010.009",
language = "English",
journal = "Biological Chemistry",
issn = "1431-6730",
publisher = "Walterde Gruyter GmbH",

}

RIS

TY - JOUR

T1 - A novel matrix metalloprotease-like enzyme (karilysin) of the periodontal pathogen Tannerella forsythia ATCC 43037

AU - Karim, Abdulkarim Y

AU - Kulczycka, Magdalena

AU - Kantyka, Tomasz

AU - Dubin, Grzegorz

AU - Jabaiah, Abeer

AU - Daugherty, Patrick S

AU - Thogersen, Ida B

AU - Enghild, Jan J

AU - Nguyen, Ky-Anh

AU - Potempa, Jan

PY - 2009

Y1 - 2009

N2 - Abstract Proteases of Tannerella forsythia, a pathogen associated with periodontal disease, are implicated as virulence factors. Here, we characterized a matrix metalloprotease (MMP)-like enzyme of T. forsythia referred to as karilysin. Full-length (without a signal peptide) recombinant karilysin (49.9 kDa) processed itself into the mature 18 kDa enzyme through sequential autoproteolytic cleavages both at N- and C-terminal profragments. The first cleavage at the Asn14-Tyr15 peptide bond generated the fully active enzyme (47.9 kDa) and subsequent truncations at the C-termini did not affect proteolytic activity. Mutation of Tyr15 to Ala generated a prokarilysin variant that processed itself into the final 18 kDa form with greatly reduced kinetics. Inactive prokarilysin with the mutated catalytic Glu residue (E136A) was processed by active karilysin at the same sites as the active enzymes. The karilysin proteolytic activity and autoprocessing were inhibited by 1,10-phenanthroline and EDTA. Calcium ions were found to be important for both activity and thermal stability of karilysin. Using the CLiPS technology, the specificity of karilysin was found to be similar to that of MMPs with preference for Leu/Tyr/Met at P1' and Pro/Ala at P3. This specificity and the ability to degrade elastin, fibrinogen and fibronectin may contribute to the pathogenicity of periodontitis.

AB - Abstract Proteases of Tannerella forsythia, a pathogen associated with periodontal disease, are implicated as virulence factors. Here, we characterized a matrix metalloprotease (MMP)-like enzyme of T. forsythia referred to as karilysin. Full-length (without a signal peptide) recombinant karilysin (49.9 kDa) processed itself into the mature 18 kDa enzyme through sequential autoproteolytic cleavages both at N- and C-terminal profragments. The first cleavage at the Asn14-Tyr15 peptide bond generated the fully active enzyme (47.9 kDa) and subsequent truncations at the C-termini did not affect proteolytic activity. Mutation of Tyr15 to Ala generated a prokarilysin variant that processed itself into the final 18 kDa form with greatly reduced kinetics. Inactive prokarilysin with the mutated catalytic Glu residue (E136A) was processed by active karilysin at the same sites as the active enzymes. The karilysin proteolytic activity and autoprocessing were inhibited by 1,10-phenanthroline and EDTA. Calcium ions were found to be important for both activity and thermal stability of karilysin. Using the CLiPS technology, the specificity of karilysin was found to be similar to that of MMPs with preference for Leu/Tyr/Met at P1' and Pro/Ala at P3. This specificity and the ability to degrade elastin, fibrinogen and fibronectin may contribute to the pathogenicity of periodontitis.

U2 - 10.1515/BC.2010.009

DO - 10.1515/BC.2010.009

M3 - Journal article

C2 - 19919176

JO - Biological Chemistry

JF - Biological Chemistry

SN - 1431-6730

ER -