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alpha1-antitrypsin + H2O
?
-
-
-
?
alpha1-proteinase inhibitor + H2O
?
-
-
-
-
?
angiotensin + H2O
?
-
-
-
-
?
factor H + H2O
?
-
cleavage yields a a factor H subfragment of approximately 50 kDa
-
-
?
immunogobulin G heavy chain + H2O
?
-
weak substrate
-
?
interleukin-1 beta + H2O
?
-
-
-
?
interleukin-1beta + H2O
?
-
-
-
?
interleukin-6 + H2O
?
-
-
-
?
Laminin + H2O
?
-
-
-
-
?
N-succinyl-AAPF-4-nitroanilide + H2O
?
synthetic substrate
-
?
N-succinyl-AAPL-4-nitroanilide + H2O
?
-
synthetic substrate
-
?
N-succinyl-AAPN-4-nitroanilide + H2O
?
-
synthetic substrate
-
?
N-succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine-4-nitroanilide + H2O
N-succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine + 4-nitroaniline
PrcA + H2O
PrcA1 + PrcA2
-
-
two auxillary polypeptides
-
?
protein factor H + H2O
?
-
-
-
-
?
serum albumin + H2O
?
-
-
-
-
?
Substance P + H2O
?
-
-
-
-
?
Suc-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
Suc-Ala-Ala-Pro-Phe + p-nitroaniline
-
-
-
-
?
succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine-4-nitroanilide + H2O
succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine + 4-nitroaniline
transferrin + H2O
?
-
-
-
-
?
tumor necrosis factor alpha + H2O
?
-
-
-
?
additional information
?
-
Fibrinogen + H2O
?
-
-
-
-
?
Fibrinogen + H2O
?
-
-
-
?
Fibronectin + H2O
?
-
-
-
?
Fibronectin + H2O
?
-
-
-
?
Fibronectin + H2O
?
-
-
-
-
?
Fibronectin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
N-succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine-4-nitroanilide + H2O
N-succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine + 4-nitroaniline
-
-
-
?
N-succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine-4-nitroanilide + H2O
N-succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine + 4-nitroaniline
-
-
-
-
?
N-succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine-4-nitroanilide + H2O
N-succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine + 4-nitroaniline
-
-
-
?
N-succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine-4-nitroanilide + H2O
N-succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine + 4-nitroaniline
-
-
-
-
?
N-succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine-4-nitroanilide + H2O
N-succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine + 4-nitroaniline
-
-
-
?
N-succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine-4-nitroanilide + H2O
N-succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine + 4-nitroaniline
-
-
-
?
N-succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine-4-nitroanilide + H2O
N-succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine + 4-nitroaniline
-
-
-
-
?
succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine-4-nitroanilide + H2O
succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine + 4-nitroaniline
-
-
-
-
?
succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine-4-nitroanilide + H2O
succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine + 4-nitroaniline
-
-
-
-
?
Type IV collagen + H2O
?
-
-
-
-
?
Type IV collagen + H2O
?
-
weak substrate
-
?
additional information
?
-
-
specificity for peptide bonds containing phenylalanine and proline at the P1 and P2 positions
-
?
additional information
?
-
involved in localization and oligomerization of the major surface protein
-
?
additional information
?
-
-
major role in structural organization of the outer sheath of Treponema
-
?
additional information
?
-
-
no degradation of native type I collagen
-
-
?
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Abscess
The Treponema denticola FhbB Protein Is a Dominant Early Antigen That Elicits FhbB Variant-Specific Antibodies That Block Factor H Binding and Cleavage by Dentilisin.
Carcinogenesis
Treponema denticola chymotrypsin-like proteinase may contribute to orodigestive carcinogenesis through immunomodulation.
Carcinoma
Treponema denticola chymotrypsin-like proteinase is present in early-stage mobile tongue squamous cell carcinoma and related to the clinicopathological features.
Carcinoma, Squamous Cell
Treponema denticola chymotrypsin-like proteinase is present in early-stage mobile tongue squamous cell carcinoma and related to the clinicopathological features.
Infections
The Treponema denticola FhbB Protein Is a Dominant Early Antigen That Elicits FhbB Variant-Specific Antibodies That Block Factor H Binding and Cleavage by Dentilisin.
Neoplasms
The Treponema denticola surface protease dentilisin degrades interleukin-1beta (IL-1beta), IL-6, and tumor necrosis factor alpha.
Neoplasms
Treponema denticola chymotrypsin-like protease as associated with HPV-negative oropharyngeal squamous cell carcinoma.
Neoplasms
Treponema denticola chymotrypsin-like proteinase is present in early-stage mobile tongue squamous cell carcinoma and related to the clinicopathological features.
Neoplasms
Treponema denticola chymotrypsin-like proteinase may contribute to orodigestive carcinogenesis through immunomodulation.
Peri-Implantitis
Periodontitis and peri-implantitis tissue levels of Treponema denticola-CTLP and its MMP-8 activating ability.
Periodontal Diseases
Analysis of the complement sensitivity of oral treponemes and the potential influence of FH binding, FH cleavage and dentilisin activity on the pathogenesis of periodontal disease.
Periodontal Diseases
Approaches to Understanding Mechanisms of Dentilisin Protease Complex Expression in Treponema denticola.
Periodontal Diseases
Characterization of the Treponema denticola Virulence Factor Dentilisin.
Periodontal Diseases
Conservation and revised annotation of the Treponema denticola prcB-prcA-prtP locus encoding the dentilisin (CTLP) protease complex.
Periodontal Diseases
The Treponema denticola FhbB Protein Is a Dominant Early Antigen That Elicits FhbB Variant-Specific Antibodies That Block Factor H Binding and Cleavage by Dentilisin.
Periodontal Diseases
Treponema denticola dentilisin triggered TLR2/MyD88 activation upregulates a tissue destructive program involving MMPs via Sp1 in human oral cells.
Periodontal Diseases
Treponema denticola PrcB is required for expression and activity of the PrcA-PrtP (dentilisin) complex.
Periodontal Pocket
Analysis of the complement sensitivity of oral treponemes and the potential influence of FH binding, FH cleavage and dentilisin activity on the pathogenesis of periodontal disease.
Periodontitis
Periodontitis and peri-implantitis tissue levels of Treponema denticola-CTLP and its MMP-8 activating ability.
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malfunction
inactivation of dentilisin abolishes the coaggregation activity
malfunction
-
inactivation of dentilisin abolishes the coaggregation activity
-
malfunction
-
inactivation of dentilisin abolishes the coaggregation activity
-
malfunction
-
inactivation of dentilisin abolishes the coaggregation activity
-
physiological function
-
Treponema denticola acylated outer membrane PrtP protease complex induces both activation of MMP-2 and generation of fibronectin fragments in human PDL cell culture supernatants
physiological function
-
negative complement regulatory protein factor H bound to the FhbB protein on the surface of Treponema denticola cell curface to avoid complement-mediated cell killing. The enzyme activity triggers localized dysregulation of complement activation in periodontal pockets
physiological function
the enzyme dentilisin is a surface protease complex that has a significant role in Treponema denticola-host interactions in periodontal disease
physiological function
-
the enzyme is involved in biofilm formation and, within a high-molecular-mass complex on the cell surface, mediates adherence of Treponema denticola to other potential periodontal pathogens, Porphyromonas gingivalis, Fusobacterium nucleatum, Prevotella intermedia, and Parvimonas micra. The enzyme's protease activity is not required for the interaction, but the enzyme expression is critical for dual-species biofilm formation, overview
physiological function
the enzyme is required for formation of the so called Red complex between Porphyromonas gingivalis, Treponema denticola, and Tannerella forsythia, although the protease activity of the enzyme is not necessary. Treponema denticola strain ATCC 33520 shows low level of coaggregation
physiological function
the enzyme is required for formation of the so called Red complex between Porphyromonas gingivalis, Treponema denticola, and Tannerella forsythia, although the protease activity of the enzyme is not necessary. Treponema denticola strain ATCC 33521 shows only a trace level of coaggregation
physiological function
the enzyme is required for formation of the socalled Red complex between Porphyromonas gingivalis, Treponema denticola, and Tannerella forsythia, although the protease activity of the enzyme is not necessary. Treponema denticola strain ATCC 35405 shows a higher level of coaggregation
physiological function
-
Treponema denticola acylated outer membrane PrtP protease complex induces both activation of MMP-2 and generation of fibronectin fragments in human PDL cell culture supernatants
-
physiological function
-
the enzyme is required for formation of the so called Red complex between Porphyromonas gingivalis, Treponema denticola, and Tannerella forsythia, although the protease activity of the enzyme is not necessary. Treponema denticola strain ATCC 33520 shows low level of coaggregation
-
physiological function
-
the enzyme is required for formation of the so called Red complex between Porphyromonas gingivalis, Treponema denticola, and Tannerella forsythia, although the protease activity of the enzyme is not necessary. Treponema denticola strain ATCC 33521 shows only a trace level of coaggregation
-
physiological function
-
the enzyme is required for formation of the socalled Red complex between Porphyromonas gingivalis, Treponema denticola, and Tannerella forsythia, although the protease activity of the enzyme is not necessary. Treponema denticola strain ATCC 35405 shows a higher level of coaggregation
-
physiological function
-
the enzyme is required for formation of the so called Red complex between Porphyromonas gingivalis, Treponema denticola, and Tannerella forsythia, although the protease activity of the enzyme is not necessary. Treponema denticola strain ATCC 33521 shows only a trace level of coaggregation
-
physiological function
-
the enzyme is required for formation of the socalled Red complex between Porphyromonas gingivalis, Treponema denticola, and Tannerella forsythia, although the protease activity of the enzyme is not necessary. Treponema denticola strain ATCC 35405 shows a higher level of coaggregation
-
physiological function
-
the enzyme is involved in biofilm formation and, within a high-molecular-mass complex on the cell surface, mediates adherence of Treponema denticola to other potential periodontal pathogens, Porphyromonas gingivalis, Fusobacterium nucleatum, Prevotella intermedia, and Parvimonas micra. The enzyme's protease activity is not required for the interaction, but the enzyme expression is critical for dual-species biofilm formation, overview
-
physiological function
-
the enzyme dentilisin is a surface protease complex that has a significant role in Treponema denticola-host interactions in periodontal disease
-
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additional information
-
dentilisin-deficient mutant K1
additional information
dentilisin-deficient mutant K1
additional information
-
mutant of the 43000 protein lacking detectable dentilisin activity, dentilisn protein degraded in the mutant
additional information
in the isogenic CTLP mutant strain, CKE, chymotrypsin-like activity is reduced more than 90% compared to that in the wild type and fibrinogen binding and hydrolysis are ablated, the isogenic mutant strain MHE shows levels of CTLP reduced 40% relative to those in the wild type and exhibits correspondingly reduced levels of fibrinogen binding and proteolysis
additional information
-
in the isogenic CTLP mutant strain, CKE, chymotrypsin-like activity is reduced more than 90% compared to that in the wild type and fibrinogen binding and hydrolysis are ablated, the isogenic mutant strain MHE shows levels of CTLP reduced 40% relative to those in the wild type and exhibits correspondingly reduced levels of fibrinogen binding and proteolysis
additional information
-
construction of dentilisin deletion mutants of strain ATCC 35405
additional information
construction of dentilisin deletion mutants of strain ATCC 35405
additional information
-
construction of dentilisin deletion mutants of strain ATCC 35520
additional information
construction of dentilisin deletion mutants of strain ATCC 35520
additional information
-
construction of dentilisin deletion mutants of strain ATCC 35521
additional information
construction of dentilisin deletion mutants of strain ATCC 35521
additional information
-
construction of dentilisin deletion mutants of strain ATCC 35405
-
additional information
-
construction of dentilisin deletion mutants of strain ATCC 35521
-
additional information
-
construction of dentilisin deletion mutants of strain ATCC 35520
-
additional information
-
construction of dentilisin deletion mutants of strain ATCC 35405
-
additional information
-
construction of dentilisin deletion mutants of strain ATCC 35521
-
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Ishihara, K.; Miura, T.; Kuramitsu, H.K.; Okuda, K.
Characterization of the Treponema denticola prtP gene encoding a prolyl-phenylalanine-specific protease (dentilisin)
Infect. Immun.
64
5178-5186
1996
Treponema denticola
brenda
Ishihara, K.; Kuramitsu, H.K.; Miura, T.; Okuda, K.
Dentilisin activity affects the organization of the outer sheath of Treponema denticola
J. Bacteriol.
180
3837-3844
1998
Treponema denticola
brenda
Lee, S.Y.; Bian, X.L.; Wong, G.W.; Hannam, P.M.; McBride, B.C.; Fenno, J.C.
Cleavage of Treponema denticola PrcA polypeptide to yield protease complex-associated proteins Prca1 and Prca2 is dependent on PrtP
J. Bacteriol.
184
3864-3870
2002
Treponema denticola (Q8VP59)
brenda
Ishihara, K.; Kuramitsu, H.K.; Okuda, K.
A 43-kDa protein of Treponema denticola is essential for dentilisin activity
FEMS Microbiol. Lett.
232
181-188
2004
Treponema denticola
brenda
Uitto, V.
Trepolisin
Handbook of Proteolytic Enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , Eds. ) Academic Press
2
1813-1815
2004
Treponema denticola
-
brenda
Miyamoto, M.; Ishihara, K.; Okuda, K.
The Treponema denticola surface protease dentilisin degrades interleukin-1 beta (IL-1 beta), IL-6, and tumor necrosis factor alpha
Infect. Immun.
74
2462-2467
2006
Treponema denticola, Treponema denticola (P96091)
brenda
Bamford, C.V.; Fenno, J.C.; Jenkinson, H.F.; Dymock, D.
The chymotrypsin-like protease complex of Treponema denticola ATCC 35405 mediates fibrinogen adherence and degradation
Infect. Immun.
75
4364-4372
2007
Treponema denticola (P96091), Treponema denticola
brenda
McDowell, J.V.; Huang, B.; Fenno, J.C.; Marconi, R.T.
Analysis of a unique interaction between the complement regulatory protein factor H and the periodontal pathogen Treponema denticola
Infect. Immun.
77
1417-1425
2009
Treponema denticola
brenda
Godovikova, V.; Wang, H.T.; Goetting-Minesky, M.P.; Ning, Y.; Capone, R.F.; Slater, C.K.; Fenno, J.C.
Treponema denticola PrcB is required for expression and activity of the PrcA-PrtP (dentilisin) complex
J. Bacteriol.
192
3337-3344
2010
Treponema denticola
brenda
Miao, D.; Fenno, J.C.; Timm, J.C.; Joo, N.E.; Kapila, Y.L.
The Treponema denticola chymotrypsin-like protease dentilisin induces matrix metalloproteinase-2-dependent fibronectin fragmentation in periodontal ligament cells
Infect. Immun.
79
806-811
2011
Treponema denticola, Treponema denticola MHE
brenda
Sano, Y.; Okamoto-Shibayama, K.; Tanaka, K.; Ito, R.; Shintani, S.; Yakushiji, M.; Ishihara, K.
Dentilisin involvement in coaggregation between Treponema denticola and Tannerella forsythia
Anaerobe
30
45-50
2014
Treponema denticola, Treponema denticola (P96091), Treponema denticola ATCC 35405, Treponema denticola ATCC 35520 (P96091), Treponema denticola ATCC 35521
brenda
Cogoni, V.; Morgan-Smith, A.; Fenno, J.C.; Jenkinson, H.F.; Dymock, D.
Treponema denticola chymotrypsin-like proteinase (CTLP) integrates spirochaetes within oral microbial communities
Microbiology
158
759-770
2012
Treponema denticola, Treponema denticola ATCC 35405
brenda
Goetting-Minesky, M.P.; Godovikova, V.; Li, J.J.; Seshadrinathan, S.; Timm, J.C.; Kamodia, S.S.; Fenno, J.C.
Conservation and revised annotation of the Treponema denticola prcB-prcA-prtP locus encoding the dentilisin (CTLP) protease complex
Mol. Oral Microbiol.
28
181-191
2013
Treponema denticola (P96091), Treponema denticola, Treponema denticola ATCC 35405 (P96091)
brenda
Miller, D.P.; McDowell, J.V.; Bell, J.K.; Goetting-Minesky, M.P.; Fenno, J.C.; Marconi, R.T.
Analysis of the complement sensitivity of oral treponemes and the potential influence of FH binding, FH cleavage and dentilisin activity on the pathogenesis of periodontal disease
Mol. Oral Microbiol.
29
194-207
2014
Treponema denticola
brenda
Kylmae, A.K.; Jouhi, L.; Listyarifah, D.; Mohamed, H.; Maekitie, A.; Remes, S.M.; Haglund, C.; Atula, T.; Nieminen, M.T.; Sorsa, T.; Hagstroem, J.
Treponema denticola chymotrypsin-like protease as associated with HPV-negative oropharyngeal squamous cell carcinoma
Br. J. Cancer
119
89-95
2018
Treponema denticola (P96091), Treponema denticola
brenda