Any feedback?
No. of entries
Information on EC 3.4.21.B21 - trepolisin
for references in articles please use BRENDA:EC3.4.21.B21
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Old data from external sources may still be available.
Please check here for current data: EC unknown
Please check here for current data: EC unknown
preliminary BRENDA-supplied EC number
EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.21 Serine endopeptidases
3.4.21.B21 trepolisin
The expected taxonomic range for this enzyme is: Treponema denticola
- 3.4.21.B21
- treponema
- denticola
- periodontal
-
gingival
-
spirochete
-
sheath
-
evasion
-
subgingival
-
ligament
-
coaggregation
-
periodontium
- prca
-
crevice
-
porphyromonas
-
dysbiosis
-
periopathogen
- diagnostics
- medicine
Reaction Schemes
showchymotrypsin-like protease, cleaves peptide bonds containing phenylalanine and proline
Synonyms
dentilisin, td-ctlp, prtp protease, td chymotrypsin-like protease, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
chymotrypsin-like protease
chymotrypsin-like proteinase
CTLP
dentilisin
PrtP
PrtP protease
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
chymotrypsin-like protease, cleaves peptide bonds containing phenylalanine and proline
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
cleavage of C-N-linkage
hydrolysis of peptide bond
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
212763-27-4
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
factor H + H2O
?
-
Substrates: cleavage yields a a factor H subfragment of approximately 50 kDa
Products: -
Products: -
?
immunogobulin G heavy chain + H2O
?
-
Substrates: weak substrate
Products: -
Products: -
?
N-succinyl-AAPF-4-nitroanilide + H2O
?
Substrates: synthetic substrate
Products: -
Products: -
?
N-succinyl-AAPL-4-nitroanilide + H2O
?
-
Substrates: synthetic substrate
Products: -
Products: -
?
N-succinyl-AAPN-4-nitroanilide + H2O
?
-
Substrates: synthetic substrate
Products: -
Products: -
?
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
-
Substrates: -
Products: two auxillary polypeptides
Products: two auxillary polypeptides
?
Suc-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
Suc-Ala-Ala-Pro-Phe + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine-4-nitroanilide + H2O
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
-
Substrates: -
Products: -
Products: -
?
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
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
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
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
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
Substrates: -
Products: -
Products: -
?
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
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine-4-nitroanilide + H2O
succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine-4-nitroanilide + H2O
succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: specificity for peptide bonds containing phenylalanine and proline at the P1 and P2 positions
Products: -
Products: -
?
additional information
?
-
Substrates: involved in localization and oligomerization of the major surface protein
Products: -
Products: -
?
additional information
?
-
-
Substrates: major role in structural organization of the outer sheath of Treponema
Products: -
Products: -
?
additional information
?
-
-
Substrates: no degradation of native type I collagen
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
PrcA + H2O
PrcA1 + PrcA2
-
Substrates: -
Products: two auxillary polypeptides
Products: two auxillary polypeptides
?
additional information
?
-
Substrates: involved in localization and oligomerization of the major surface protein
Products: -
Products: -
?
additional information
?
-
-
Substrates: major role in structural organization of the outer sheath of Treponema
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
not inhibited by Tos-Lys-CH2Cl, alpha1-proteinase inhibitor and pepstatin
-
PMSF
the inhibitor treatment leads to inactivation of the enzymes proteolytic activity, but has no effect on adherence of Treponema denticola to Porphyromonas gingivalis and Tannerella forsythia; the inhibitor treatment leads to inactivation of the enzymes proteolytic activity, but has no effect on adherence of Treponema denticola to Porphyromonas gingivalis and Tannerella forsythia
PMSF
-
the inhibitor treatment leads to over 95% inactivation of the enzymes proteolytic activity, but has no effect on adherence of Treponema denticola to the biofilm and Porphyromonas gingivalis, Fusobacterium nucleatum, Prevotella intermedia, and Parvimonas micra
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme activity of diverse strains with cell-bound substrate protein factor H, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.42
-
72000 Da and 38000 Da protein, calculated from nucleic acid sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
diverse strains, i.e. 35405, MS25, 33520, N17A1, GM-1, SP48, SP55, SP54, SP50, SP49, SP72, 35404, SP64, 33521, CF171, and CF170
-
-
brenda
gene prtP from strain ATCC 35405; gene prtP, the enzyme is encoded in the prcB-prcA-prtP operon
UniProt
brenda
gene prtP from strain ATCC 35405; gene prtP, the enzyme is encoded in the prcB-prcA-prtP operon
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
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
-
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 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 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
-
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
-
CTLP can activate the host pro-MMP-8 enzyme. Tissue protein levels of MMP-8 and CTLP do not seem to be changed in peri-implantitis and in periodontitis
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 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 dentilisin is a surface protease complex that has a significant role in Treponema denticola-host interactions in periodontal disease
-
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 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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
38000
-
three bands at 72000 Da, 43000 Da and 38000 Da after boiling, SDS-PAGE
43000
72000
43000
-
three bands at 72000 Da, 43000 Da and 38000 Da after boiling, SDS-PAGE
43000
-
protein located in the 3' region of the prcA gene upstream of the dentilisin gene
72000
-
three bands at 72000 Da, 43000 Da and 38000 Da after boiling, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
polymer
polymer
-
x * 72000 + x * 38000 + x * 43000, 72000 Da active protease associates with smaller proteins, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
rapidly purified by sonication, SDS-PAGE, gel filtration, pressure filtration, 101fold purified by ion-exchange chromatography followed by gel filtration
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene prtP, the enzyme is encoded in the prcB-prcA-prtP operon, DNA and amino acid sequence determination and analysis, sequence comparisons of different Treponema denticola strains, phylogenetic analysis, cloning in Escherichia coli strain JM109, expression of His6-tagged enzyme in Escherichia coli strain Rosetta(DE3)/pLysS
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
PrcB is required for native expression of PrtP, PrcB is a PrtP-binding lipoprotein that stabilizes the PrtP polypeptide during localization to the outer membrane
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
Treponema denticola chymotrypsin-like protease is associated with human papillomavirus-negative oropharyngeal squamous cell carcinoma
medicine
additional information
medicine
Treponema denticola exerts a pathogenic effect on periodontal tissue via local dysregulation of inflammatory cytokines by dentilisin
medicine
-
CTLP can activate the host pro-MMP-8 enzyme. Tissue protein levels of MMP-8 and CTLP do not seem to be changed in peri-implantitis and in periodontitis
additional information
-
contributes to tissue invasion and lysis of host cells, important in migration of the organism through basement membrane, cytopathic effects on epithelial cells, able to trigger release of polymorphonuclear leukocyte granules and activates latent matrix metalloproteinases
additional information
-
43000 protein involved in the stabilization of the dentilisn protein
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Petain, S.; Kasnak, G.; Firatli, E.; Tervahartiala, T.; Guersoy, U.K.; Sorsa, T.
Periodontitis and peri-implantitis tissue levels of Treponema denticola-CTLP and its MMP-8 activating ability
Acta Histochem.
123
151767
2021
Treponema denticola
brenda
EXTERNAL LINKS (specific for EC-Number 3.4.21.B21)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
