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Information on EC 3.4.22.B8 - Tpr proteinase (Porphyromonas gingivalis) and Organism(s) Porphyromonas gingivalis and UniProt Accession P25806

for references in articles please use BRENDA:EC3.4.22.B8
preliminary BRENDA-supplied EC number
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Porphyromonas gingivalis
UNIPROT: P25806
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Word Map
  • 3.4.22.B8
  • caspase-8
  • apaf-1
  • apoptosome
  • procaspase-9
  • bcl-xl
  • z-lehd-fmk
  • caspase-9-specific
  • caspase-9-mediated
The taxonomic range for the selected organisms is: Porphyromonas gingivalis
The expected taxonomic range for this enzyme is: Porphyromonas gingivalis
Synonyms
C02.022, Tpr peptidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C02.022
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
37353-41-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Azocoll + H2O
?
show the reaction diagram
-
-
-
?
Bovine serum albumin + H2O
?
show the reaction diagram
-
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
?
denatured collagen + H2O
?
show the reaction diagram
no activity on native collagen
-
-
?
Suc-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
both autoprocessing and activity are dependent on calcium concentrations above 1 mM. Presence of Calcium also stabilizes the Tpr structure and renders the protein fully resistant to proteolytic degradation by gingipains
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
inhibitory concentration: 15-20 mM
Co2+
inhibitory below 5 mM
Cu2+
inhibitory below 5 mM
Fe2+
inhibitory below 5 mM
Hg2+
inhibitory below 5 mM
Mg2+
inhibitory concentration: 15-20 mM
Mn2+
inhibitory concentration: 5-10 mM
Ni2+
inhibitory below 5 mM
Zn2+
inhibitory below 5 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
stimulates
cysteine
stimulates
dithiothreitol
stimulates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0147
Suc-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
pH 7.5, 37°C
0.0232
Z-Phe-Arg-7-amido-4-methylcoumarin
pH 7.5, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0011
Suc-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
pH 7.5, 37°C
0.018
Z-Phe-Arg-7-amido-4-methylcoumarin
pH 7.5, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9
recombinant enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
inactive at or below 20 C when azocoll is the substrate, inactive at 90 C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
protein is associated with the bacterial outer membrane
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
64000
x * 64000, SDS-PAGE
55000
-
2 * 55000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 55000
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
the 55-kDa Tpr inactive zymogen proteolytically processes itself into active forms of 48, 37, and 33 kDa via sequential truncations at the N terminus
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
controll of trp expression in Escherichia coli appears to be quite different from expression in Porphyra gingivalis
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bourgeau, G.; Lapointe, H.; Peloquin, P.; Mayrand, D.
Cloning, expression, and sequencing of a protease gene (tpr) from Porphyromonas gingivalis W83 in Escherichia coli
Infect. Immun.
60
3186-3192
1992
Porphyromonas gingivalis (P25806), Porphyromonas gingivalis W83 (P25806)
Manually annotated by BRENDA team
Park, Y.; Lu, B.; mazur, C.; McBride, B.C.
Inducible expression of a Porphyromonas gingivalis W83 membrane-associated protease
Infect. Immun.
65
1101-1104
1997
Porphyromonas gingivalis
Manually annotated by BRENDA team
Lu, B.; McBride, B.C.
Expression of the trp gene of Porphyromonas gingivalis is regulated by peptide nutrients
Infect. Immun.
66
5147-5156
1998
Porphyromonas gingivalis
Manually annotated by BRENDA team
Staniec, D.; Ksiazek, M.; Thogersen, I.; Enghild, J.; Sroka, A.; Bryzek, D.; Bogyo, M.; Abrahamson, M.; Potempa, J.
Calcium regulates the activity and structural stability of TPR, a bacterial calpain-like peptidase
J. Biol. Chem.
290
27248-27260
2015
Porphyromonas gingivalis (P25806), Porphyromonas gingivalis ATCC BAA-308 (P25806)
Manually annotated by BRENDA team