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Information on EC 3.4.22.47 - gingipain K and Organism(s) Porphyromonas gingivalis and UniProt Accession B2RLK2
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3.4.22.47 gingipain KSpecify your search results
Word Map
- 3.4.22.47
- gingivalis
- porphyromonas
- periodontal
-
gingipains
- arg-gingipains
- proteinases
-
arginine-specific
-
crevicular
-
keystone
- hrgpa
-
subgingival
- molecular biology
-
black-pigmented
-
gingivalis-induced
-
coaggregation
- medicine
-
arg-specific
-
gingipain-deficient
The taxonomic range for the selected organisms is: Porphyromonas gingivalis
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
lys-gingipain, gingipain k, lysine-specific gingipain, lysine gingipain, lysine-specific proteinase, k-gingipain, porphypain, lysine-specific gingipain proteinase, lys-specific cysteine proteinase gingipain, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
HbR
-
adhesin domain of gingipain which is able to bind heme as an iron nutrient source for Porphyromonas gingivalis
KGP
Lys-gingipain
PrtP proteinase
-
-
-
-
KGP
-
-
KGP
-
gingipains are classified according to their cleavage-site specificity into Kgps, lysine-specific gingipains, and Rgps, arginine-specific gingipains
KGP
-
high molecular weight form containing both catalytic and adhesin subunit
Lys-gingipain
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
endopeptidase with strict specificity for lysyl bonds
active site structure, role of the Sn binding pocket, molecular basis for substrate specificity
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
159745-69-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
elafin + H2O
?
all three gingipains have the ability to degrade elafin (endogenous inhibitor secreted by epithelial cells)
-
-
?
acetyl-lysine-4-nitroanilide + H2O
acetyl-lysine + 4-nitroaniline
-
-
-
-
?
acid-soluble human placental type I collagen + H2O
fragments of acid-soluble human placental type I collagen
-
-
-
-
?
adrenocorticotropic hormone fragment 11-24 + H2O
fragments of adrenocorticotropic hormone fragment 11-24
-
-
-
?
benzyloxycarbonyl-L-Lys-p-nitroanilide + H2O
benzyloxycarbonyl-L-Lys + p-nitroaniline + H2O
bovine serum albumin + H2O
fragments of bovine serum albumin
-
-
-
-
?
bradykinin + H2O
fragments of bradykinin
-
together with gingipain R, gingipain K induces vascular permeability enhancement in human plasma by cleaving bradykinin from high molecular weight kininogen
-
?
CD46 + H2O
?
-
recombinant CD46 is degraded by Lys-gingipain in a dose-dependent manner
-
-
?
focal adhesion kinase + H2O
?
-
Kgp is responsible for degradation of integrin-related molecules
-
-
?
haptoglobin + H2O
fragments of haptoglobin
-
human serum haptoglobin
-
?
hemoglobin + H2O
fragments of hemoglobin
-
human serum hemoglobin
-
?
hemopexin + H2O
fragments of hemopexin
-
human serum hemopexin
-
?
IgG1 + H2O
?
-
The heavy chain of IgG1 is cleaved at a single site within the hinge region, generating Fab and Fc fragments
-
-
?
IgG3 + H2O
?
-
IgG3 is cleaved within the heavy chain and at several sites around the CH2 region
-
-
?
Met-Lys-bradykinin + H2O
fragments of Met-Lys-bradykinin
-
-
-
?
monocyte chemotactic protein 1 + H2O
fragments of monocyte chemotactic protein 1
-
degradation of human monocyte chemotactic protein 1 in Porphyromonas gingivalis-infected human umbilical vein endothelial cells
-
?
N-(p-tosyl)-Gly-Pro-Lys-4-nitroanilide + H2O
N-(p-tosyl)-Gly-Pro-Lys + 4-nitroaniline
-
-
-
-
?
N-4-tosyl-Gly-Pro-Lys-4-nitroanilide + H2O
N-4-tosyl-Gly-Pro-Lys + 4-nitroaniline
-
-
-
-
?
N-alpha-acetyl-L-lysine-4-nitroanilide + H2O
N-alpha-acetyl-L-lysine + 4-nitroaniline
-
-
-
-
?
N-alpha-acetyl-L-lysine-p-nitroanilide + H2O
N-alpha-acetyl-L-lysine + 4-nitroaniline
-
-
-
-
r
N-alpha-benzoyl-DL-lysine 4-nitroanilide + H2O
N-alpha-benzoyl-DL-lysine + 4-nitroaniline
-
-
-
-
?
N-alpha-benzyloxycarbonyl-L-lysine-4-nitroanilide + H2O
N-alpha-benzyloxycarbonyl-L-lysine + 4-nitroaniline
-
-
-
-
?
N-p-tosyl-Gly-Pro-Lys-4-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Lys + 4-nitroaniline
-
-
-
-
?
Nalpha-acetyl-L-lysine 4-nitroanilide + H2O
Nalpha-acetyl-L-lysine + 4-nitroaniline
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-lysine 4-nitroanilide + H2O
Nalpha-benzyloxycarbonyl-L-lysine + 4-nitroaniline
-
-
-
-
?
neurotensin + H2O
pGlu-Leu-Tyr-Glu-Asn-Lys + Pro-Arg-Arg-Pro-Tyr-Ile-Leu
-
-
-
?
paxillin + H2O
?
-
Kgp is responsible for degradation of integrin-related molecules
-
-
?
protease-activated receptor-2 + H2O
?
-
specific substrate for Lys-gingipain
-
-
?
t-butyl-oxycarbonyl-L-Glu-L-Lys-L-Lys-4-methyl-7-coumarylamide + H2O
t-butyl-oxycarbonyl-L-Glu-L-Lys-L-Lys + 7-amino-4-methylcoumarin
-
41% of activity with t-butyl-oxycarbonyl-L-Val-L-Leu-L-Lys-4-methyl-7-coumarylamide
-
?
t-butyl-oxycarbonyl-L-Val-L-Leu-L-Lys-4-methyl-7-coumarylamide + H2O
t-butyl-oxycarbonyl-L-Val-L-Leu-L-Lys + 7-amino-4-methylcoumarin
-
gingipain K has a stron preference for substrates containing Lys in the p1 site
-
?
t-butyloxycarbonyl-Val-Leu-Lys-Phe-Arg-4-methyl-7-coumarylamide
t-butyl-oxycarbonyl-Val-Leu-Lys + Phe-Arg-4-methyl-7-coumarylaminde
-
-
-
-
?
thrombomodulin + H2O
?
-
Lys-gingipain and Arg-gingipain cleave thrombomodulin in vitro
-
-
?
transferrin + H2O
fragments of transferrin
-
human serum transferrin
-
?
Val-Leu-Lys-4-nitroanilide + h2O
Val-Leu-Lys + 4-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-L-Lys-p-nitroanilide + H2O
benzyloxycarbonyl-L-Lys + p-nitroaniline + H2O
-
-
-
?
benzyloxycarbonyl-L-Lys-p-nitroanilide + H2O
benzyloxycarbonyl-L-Lys + p-nitroaniline + H2O
-
7% of activity with N-p-tosyl-Gly-Pro-Lys-p-nitroanilide
-
-
?
D-Val-Leu-Lys-p-nitroanilide + H2O
D-Val-Leu-Lys + p-nitroaniline
-
-
-
?
D-Val-Leu-Lys-p-nitroanilide + H2O
D-Val-Leu-Lys + p-nitroaniline
-
-
-
?
D-Val-Phe-Lys-p-nitroanilide + H2O
D-Val-Phe-Lys + p-nitroaniline
-
-
-
?
D-Val-Phe-Lys-p-nitroanilide + H2O
D-Val-Phe-Lys + p-nitroaniline
-
70% of activity with N-p-tosyl-Gly-Pro-Lys-p-nitroanilide
-
?
Fibrinogen + H2O
Fragments of fibrinogen
-
prominent target among plasma proteins
-
?
Fibrinogen + H2O
Fragments of fibrinogen
-
most prominent target among plasma proteins
-
-
?
Hemoglobin + H2O
?
-
degradation, the enzyme forms a complex with the outer membrane receptor HmuR required for binding and utilization of hemoglobin and hemin, overview
-
-
?
interleukin 8 + H2O
fragments of interleukin 8
-
degradation of human interleukin 8 in Porphyromonas gingivalis-infected human umbilical vein endothelial cells
-
?
interleukin-1beta + H2O
?
-
biological inactivation and degradation, low activity, cytokine degradation is mainly the result of Lys-gingipain
-
-
?
interleukin-6 + H2O
?
-
biological inactivation and degradation
-
-
?
interleukin-8 + H2O
?
-
biological inactivation and degradation
-
-
?
methemoglobin + H2O
?
-
methemoglobin, formed by treatment of oxyHb with either NaNO2 or by pre-incubation with HRgpA, is rapidly degraded by Kgp compared to oxyhemoglobin
-
-
?
methemoglobin + H2O
?
-
degradation, ligation of methemoglobin with N3-, which effectively blocks heme dissociation from the protein, prevents hemoglobin breakdown
-
-
?
methemoglobin + H2O
?
-
from horse, degradation, no activity with oxyhemoglobin
-
-
?
N-p-tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Lys + p-nitroaniline
-
-
-
?
N-p-tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Lys + p-nitroaniline
-
-
-
?
N-p-tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Lys + p-nitroaniline
-
gingipain K cleaves specifically on the C-terminal side of peptide substrates
-
?
osteoprotegerin + H2O
?
-
digestion, enhanced osteoclastogenesis by Kgp, in co-cultures of mouse bone-marrow cells and osteoblasts, formation of multinucleated osteoclasts induced by 1alpha,25-dihydroxyvitamin D3 is augmented by Kgp. The specific enzymatic activity of Kgp is necessary for osteoclast formation, overview
-
-
?
TNFalpha + H2O
?
-
degradation, leading to inhibition of biological functions of TNFalpha, overview
-
-
?
additional information
?
-
-
a combination of both arginine- and lysine-specific gingipain activity is necessary for the generation of the micro-oxo bishaem-containing pigment from haemoglobin, interaction with oxyhemoglobin, overview
-
-
?
additional information
?
-
-
gingipain K adds to gingipain R-mediated coaggregation of Porphyromonas gingivalis with other oral bacteria, it is a virulence factor, overview
-
-
?
additional information
?
-
-
gingipains are essential for bacterial virulence and survival
-
-
?
additional information
?
-
-
the C-terminal domains of the gingipain K polyprotein are necessary for assembly of the active enzyme and expression of associated activities
-
-
?
additional information
?
-
-
the enzyme degrades host iron- and heme-containing proteins, regulation of enzyme expression, overview, inhibition of gingipain increases the hmuR gene expression encoding the heme/hemoglobin receptor HmuR, and decreases the cell growth in the early and middle stages, but not in the late stages, hmuR expression inhibition decreases enzyme expression
-
-
?
additional information
?
-
-
the enzyme inactivates a cell surface ligand on Porphyromonas gingivalis that induces TLR2-and TLR4-independent signaling involving CD25, but has no effect on TLR2-and TLR4-dependent signaling, overview
-
-
?
additional information
?
-
-
role of the Sn binding pocket, molecular basis for substrate specificity, overview
-
-
?
additional information
?
-
-
extracellular gingipain protease activities cause a lack of secondary cytokine response in human cells after challenge with live Porphyromonas gingivalis
-
-
?
additional information
?
-
-
gingipains are considered to be key virulence factors of the bacterium in relation to periodontal diseases. Kgp suppresses interleukin-8 production in human HSC-2 epithelial cells requiring both the hemagglutinin and the enzymic domains. Suppression of IL-8 resultes in attenuation of the cellular recognition of bacteria, and as a consequence, sustain chronic inflammation
-
-
?
additional information
?
-
-
gingipains are cysteine proteinases and virulence factors of Porphyromonas gingivalis, the major causative bacterium of periodontal disease. Gingipains stimulate interleukin-8 secretion from human THP-1 cells, which is completely inhibited by proteinase inhibitors of gingipain and is increased in the presence of pathogen-associated molecular patterns, PAMPs. The synergism of gingipain HRgpA and PAMPs stimulates interleukin IL-6, and monocyte chemoattractant protein MCP-1 secretion, overview
-
-
?
additional information
?
-
-
gingipains are key virulence determinants of Porphyromonas gingivalis and play a crucial role in pathogenicity
-
-
?
additional information
?
-
-
gingipains reduce cyclin expression and cause early G1 arrest, leading to the inhibition of cellular proliferation in murine ST2 osteoblastic/stromal cells, overview
-
-
?
additional information
?
-
-
the membrane protein PG27, encoded by gene PG0027, is essential for the secretion of gingipains, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
elafin + H2O
?
all three gingipains have the ability to degrade elafin (endogenous inhibitor secreted by epithelial cells)
-
-
?
bradykinin + H2O
fragments of bradykinin
-
together with gingipain R, gingipain K induces vascular permeability enhancement in human plasma by cleaving bradykinin from high molecular weight kininogen
-
-
?
Fibrinogen + H2O
Fragments of fibrinogen
-
most prominent target among plasma proteins
-
-
?
focal adhesion kinase + H2O
?
-
Kgp is responsible for degradation of integrin-related molecules
-
-
?
Hemoglobin + H2O
?
-
degradation, the enzyme forms a complex with the outer membrane receptor HmuR required for binding and utilization of hemoglobin and hemin, overview
-
-
?
interleukin-1beta + H2O
?
-
biological inactivation and degradation, low activity, cytokine degradation is mainly the result of Lys-gingipain
-
-
?
interleukin-6 + H2O
?
-
biological inactivation and degradation
-
-
?
interleukin-8 + H2O
?
-
biological inactivation and degradation
-
-
?
methemoglobin + H2O
?
-
degradation, ligation of methemoglobin with N3-, which effectively blocks heme dissociation from the protein, prevents hemoglobin breakdown
-
-
?
monocyte chemotactic protein 1 + H2O
fragments of monocyte chemotactic protein 1
-
degradation of human monocyte chemotactic protein 1 in Porphyromonas gingivalis-infected human umbilical vein endothelial cells
-
-
?
osteoprotegerin + H2O
?
-
digestion, enhanced osteoclastogenesis by Kgp, in co-cultures of mouse bone-marrow cells and osteoblasts, formation of multinucleated osteoclasts induced by 1alpha,25-dihydroxyvitamin D3 is augmented by Kgp. The specific enzymatic activity of Kgp is necessary for osteoclast formation, overview
-
-
?
paxillin + H2O
?
-
Kgp is responsible for degradation of integrin-related molecules
-
-
?
protease-activated receptor-2 + H2O
?
-
specific substrate for Lys-gingipain
-
-
?
TNFalpha + H2O
?
-
degradation, leading to inhibition of biological functions of TNFalpha, overview
-
-
?
interleukin 8 + H2O
fragments of interleukin 8
-
degradation of human interleukin 8 in Porphyromonas gingivalis-infected human umbilical vein endothelial cells
-
-
?
additional information
?
-
-
a combination of both arginine- and lysine-specific gingipain activity is necessary for the generation of the micro-oxo bishaem-containing pigment from haemoglobin, interaction with oxyhemoglobin, overview
-
-
?
additional information
?
-
-
gingipain K adds to gingipain R-mediated coaggregation of Porphyromonas gingivalis with other oral bacteria, it is a virulence factor, overview
-
-
?
additional information
?
-
-
gingipains are essential for bacterial virulence and survival
-
-
?
additional information
?
-
-
the C-terminal domains of the gingipain K polyprotein are necessary for assembly of the active enzyme and expression of associated activities
-
-
?
additional information
?
-
-
the enzyme degrades host iron- and heme-containing proteins, regulation of enzyme expression, overview, inhibition of gingipain increases the hmuR gene expression encoding the heme/hemoglobin receptor HmuR, and decreases the cell growth in the early and middle stages, but not in the late stages, hmuR expression inhibition decreases enzyme expression
-
-
?
additional information
?
-
-
the enzyme inactivates a cell surface ligand on Porphyromonas gingivalis that induces TLR2-and TLR4-independent signaling involving CD25, but has no effect on TLR2-and TLR4-dependent signaling, overview
-
-
?
additional information
?
-
-
extracellular gingipain protease activities cause a lack of secondary cytokine response in human cells after challenge with live Porphyromonas gingivalis
-
-
?
additional information
?
-
-
gingipains are considered to be key virulence factors of the bacterium in relation to periodontal diseases. Kgp suppresses interleukin-8 production in human HSC-2 epithelial cells requiring both the hemagglutinin and the enzymic domains. Suppression of IL-8 resultes in attenuation of the cellular recognition of bacteria, and as a consequence, sustain chronic inflammation
-
-
?
additional information
?
-
-
gingipains are cysteine proteinases and virulence factors of Porphyromonas gingivalis, the major causative bacterium of periodontal disease. Gingipains stimulate interleukin-8 secretion from human THP-1 cells, which is completely inhibited by proteinase inhibitors of gingipain and is increased in the presence of pathogen-associated molecular patterns, PAMPs. The synergism of gingipain HRgpA and PAMPs stimulates interleukin IL-6, and monocyte chemoattractant protein MCP-1 secretion, overview
-
-
?
additional information
?
-
-
gingipains are key virulence determinants of Porphyromonas gingivalis and play a crucial role in pathogenicity
-
-
?
additional information
?
-
-
gingipains reduce cyclin expression and cause early G1 arrest, leading to the inhibition of cellular proliferation in murine ST2 osteoblastic/stromal cells, overview
-
-
?
additional information
?
-
-
the membrane protein PG27, encoded by gene PG0027, is essential for the secretion of gingipains, overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-(3-phenylpropionyl)piperidine-3-(R,S)-carboxylic acid-[4-amino-1(S)-(benzothiazole-2-carbonyl)butyl] amide
-
reversible inhibition
benzyl-N-[(2S)-1-[[(3S)-7-amino-1-(benzylamino)-1,2-dioxoheptan-3-yl]amino]-5-(2-methyl-2-phenylhydrazinyl)-1,5-dioxopentan-2-yl]carbamate
i.e. KYT-36, peptide-derived, potent, bioavailable and highly selective inhibitor
benzyloxycarbonyl-L-phenylalanyl-L-lysylacyloxyketone
-
the inhibitor completely abolishes osteoclastogenesis induced by Kgp
benzyloxycarbonyl-Phe-Lys-chloromethylketone
-
i.e. z-FKck, specific for Kgp
Chlorhexidine
-
synergistic effect of Zn2+ in a 1:1 ratio of chlorhexidine and Zn2+
Chloromethyl ketones
-
development of diverse inhibitor derivatives: structure-based design, chemistry, and activity, specificity for the Sn binding pocket of the enzyme, overview
kappa-casein
-
inhibits proteolytic activity associated with Porphyromonas gingivalis whole cells, purified RgpA-Kgp proteinase-adhesin complexes, and purified RgpB proteinase. The peptide kappa-casein(109-137) exhibits synergism with Zn(II) against both Arg- and Lys-specific proteinases. Active region for inhibition is identified as kappa-casein (117-137). Kappa-casein inhibits in an uncompetitive manner
-
lactoferrin
-
inhibits both the Arg- and Lys-specific proteinase activities of Porphyromonas gingivalis whole cells by approximately 40% at 1 mg/ml and over 70% at 10 mg/ml. Lactoferrin inhibits both the Arg-specific and Lys-specific activities of purified Porphyromonas gingivalis 248 RgpA/Kgp proteinase-adhesin complexes by 96% at a concentration of 5 mg/mL
-
lysine
-
slight inhibition of coaggregation of Porphyromonas gingivalis with other oral bacteria by L-lysine and more slightly by D-lysine
N-alpha-p-tosyl-L-lysine chloromethyl ketone
-
0.1 mM, complete inhibition
Nalpha-benzoyl-Phe-Lys-chloromethyl ketone
-
a specific inhibitor of lysine gingipain
porcine pancreatic secretory trypsin inhibitor
-
i.e. PSTI porcine, a Kazal-type serine proteinase inhibitor purified from pancreas, porcine pancreatic secretory trypsin inhibitor having an essential Lys residue at the P1 position of the reactive site, and containing Tyr and Asn residues the P2' and P3' sites, specifically inhibits the activity of the Lys-specific gingipain K, whereas bovine inhibitor, possessing a Arg residue at the P1 position, exhibits activity only against the Arg-specific cysteine proteinase gingipain K, EC 3.4.22.37. The association equilibrium constant is 0.51 mM
-
rice grain extract
-
a rice protein fraction is shown to have Rgp inhibitory activities. Comprehensive affinity chromatography and MS analyses results in the identification of 4 proteins a 26 kDa globulin, a plant lipid transfer/trypsin-alpha amylase inhibitor, the RA17 seed allergen, and an alpha amylase/trypsin inhibitor proteins accounting for 90% of the inhibitory activity. Inhibitory activity against Rgp is 20fold higher than that against Kgp
-
Z-Phe-Lys-2,4,6-trimethyl-benzoyloxymethyl-ketone
-
specific inhibition of Kgp
Z-Phe-Lys-acyloxymethylketone
-
oxyhemoglobin-Kgp interactions resulting in formation of a hemoglobin hemichrome are inhibited by specific inhibitor Z-Phe-Lys-acyloxymethylketone
zFKck
-
human gingvial epithelial cells treated with Kgp-specific inhibitor leupeptin and challenged with Porphyromonas gingivalis cells do not undergo apoptosis
KYT-36
-
specific inhibition of Kgp, slightly inhibits coaggregation of Porphyromonas gingivalis with other bacteria in vivo
additional information
-
gingipains stimulate interleukin-8 secretion from human THP-1 cells, which is completely inhibited by proteinase inhibitors of gingipain and is increased in the presence of pathogen-associated molecular patterns, PAMPs, overview
-
additional information
-
in the gene PG0027, encoding protein PG27, deletion mutant 83K10, the activities of Arg-gingipain and Lys-gingipain are severely reduced, while the activities of secreted exopeptidases DPPIV, DPP-7, and PTP-A are unaffected
-
additional information
-
no inhibition by chicken ovoinhibitor III and IV domains
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cysteine
-
most effective reducing agent for activation, maximal activation at 50 mM
cysteine
-
gingipains are activated by diluting to 10 mM in 0.2 M HEPES, pH 8.0, 5 mM CaCl2 and 10 mM cysteine, and incubation at 37°C for 10 min
additional information
-
activation of gingipain R by incubation for 10 min in 200 mM Tris-HCl buffer, pH 7.6, containing 50 mM Gly-Gly, 10 mM CaCl2 and 10 mM Cys-HCl
-
additional information
-
gingipains stimulate interleukin-8 secretion from human THP-1 cells, which is completely inhibited by proteinase inhibitors of gingipain and is increased in the presence of pathogen-associated molecular patterns, PAMPs, overview
-
additional information
-
membrane protein PG27 is essential for secretion of gingipains and their extracellular activity, and is localized in both the inner and outer membranes
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
gingipain K binds hemoglobin, porphyrins and metalloporphyrins
-
additional information
additional information
-
Investigation of the enzyme kinetics of IgG proteolysis by gingipain K, using FPLC- and isothermal titration calorimetry-based assays followed by Hill plots, reveal non-Michaelis-Menten kinetics involving a mechanism of positive cooperativity
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000009
1-(3-phenylpropionyl)piperidine-3-(R,S)-carboxylic acid-[4-amino-1(S)-(benzothiazole-2-carbonyl)butyl]amide
-
-
additional information
additional information
-
inhibition kinetics
-
additional information
additional information
-
inhibition kinetics, overview
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme activity and hemoglobin/hemin binding in wild-type strain A7436 and in kgp-deficient mutant strains WS1, WS10, and WS15, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.5
-
hydrolysis of t-butyloxycarbonyl-L-Val-L-Leu-L-Lys-4-methyl-7-coumarylamide
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9.5
-
hydrolysis of t-butyl-oxycarbonyl-L-Val-L-Leu-L-Lys-4-methyl-7-coumarylamide
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
37
-
assay at
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
Porphyromonas gingivalis secretes outer membrane vesicles that contain major virulence factors, including Arg-gingipain and Lys-gingipain
-
outer membrane protein Sov paticipates in the secretion of Lys-gingipain
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
-
Porphyromonas gingivalis Lys-gingipain (Kgp) facilitates heme acquisition by HmuY (heme-binding protein)
physiological function
malfunction
-
human keratinocyte Rgp-deficient and Kgp-deficient double mutant cells do not cleave protease-activated recptor-1 and -2. The single Kgp-negative mutant cleaves protease-activated recptor-1
malfunction
-
Porphyromonas gingivalis secretes outer membrane vesicles that contain major virulence factors, including Arg-gingipain and Lys-gingipain. Kgp-null membrane vesicles enter the cells and degrade transferrin receptor, while they scarcely degrade paxillin and focal adhesion kinase
malfunction
-
Porphyromonas gingivalis triple mutant RgpA/RgpB/Kgp cells or the Lys-gingipain (Kgp) mutant K1A cells do not induce apoptosis in human gingvial epithelial cells
malfunction
-
the roles of several virulence factors in homotypic biofilm development by Porphyromonas gingivalis. A Kgp mutant formed markedly thick biofilms filled with large clumped colonies in PBS as well as in diluted trypticase soy broth. Autoaggregation is significantly increased in the Kgp mutants, with a clear association with alteration of biofilm structures under the non-proliferation condition. Results suggests that Kgp has a suppressive and regulatory role during biofilm development and acts coordinately with other virulence factors such as long (FimA) and short (Mfa) fimbriae to regulate the development of mature biofilms
malfunction
-
using Porphyromonas gingivalis null mutant KDP136 (triple mutant for RgpA/RgpB/Kgp) gingipain-sensitive ligand are identified. Two proteins encoded by protein-coding sequence PGN_0748 and PGN_0728 are obtained
physiological function
-
expression pattern of cytokines and their receptors in differentiated macrophages following exposure to active and inactive forms of the gingipains (HRgpA, RgpB and Kgp), using a cDNA array, quantitative PCR and ELISA analysis is determined. The results indicate that the adhesin subunits of the high molecular weight gingipains (HRgpA and Kgp) mediate strong upregulation of the expression of pro-inflammatory cytokines (interleukin-1beta and colony stimulatory factor) in macrophages
physiological function
-
following entry of Porphyromonas gingivalis membrane vesicles into host cells, membrane vesicle-associated gingipains degrade cellular functional molecules such as transferrin receptor and paxillin/FAK, resulting in cellular impairment, indicating that Porphyromonas gingivalis membrane vesicles are potent vehicles for transmission of virulence factors into host cells
physiological function
-
gingipains induce the degradation and inactivation of endothelial thrombomodulin which may promote vascular coagulation and inflammation
physiological function
-
live Porphyromonas gingivalis can invoke gingival epithelial cell apoptosis in a time and dose dependent manner with significant apoptosis occurring between 12 and 24 hours of challenge via a gingipain-dependent mechanism. Either arginine or lysine gingipains are necessary and sufficient factors in Porphyromonas gingivalis elicited apoptosis
physiological function
-
the K2 domain of KgP induces haemolysis of erythrocytes in a dose-dependent manner that is augmented by the blocking of anion transport
physiological function
-
using erythrocyte and its membrane as a model, it is shown that recombinant HbR expressed in Escherichia coli can inhibit heme-induced haemolysis, probably through removing heme from the heme-membrane complex and lowering free heme toxicity by mediating dimerization of heme molecules
physiological function
-
gingipain K is an IgG protease of pathophysiological importance
physiological function
-
results suggest that gingipains may have a role in the resistance of Porphyromonas gingivalis ATCC 49417 to human beta-defensin 3
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
105000
60000
105000
-
x * 105000, gingipain K-hemagglutinin complex, enzyme exists in multiple forms, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
-
x * 105000, gingipain K-hemagglutinin complex, enzyme exists in multiple forms, SDS-PAGE
additional information
-
the predominant form of gingipain K is a complex of the 60000 Da catalytic domain with hemagglutinins, enzyme is build of a prepropeptide, a catalytic domain and a hemagglutinin domain
additional information
-
the enzyme is expressed as a large precursor protein consisting of a leader sequence, a pro-fragment, a catalytic domain with a C-terminal IgG-like subdomain, and a large hemagglutinin/adhesion domain, the latter is required for proper enzyme folding
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
gingipain K is synthesized as a polyprotein precursor that contains a proteinase domain and multiple adhesin domains, this precursor is processed at distinct sites to yield active KGP
proteolytic modification
-
the enzyme is expressed as a large precursor protein consisting of a leader sequence, a pro-fragment, a catalytic domain with a C-terminal IgG-like subdomain, and a large hemagglutinin/adhesion domain, the enzyme cleaves itself autocatalytically
proteolytic modification
gingipain K is secreted as a zymogen. It is inhibited by a pro-domain that is removed during extracellular activation. The isolated 209-residue pro-domain is a boomerang-shaped all-beta protein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting-drop vapor diffusion method, high-resolution (1.20 A) complex structure of the enzyme with KYT-36. Sub-nanomolar inhibition of Kgp is achieved by tight binding to the active-site cleft, which is covered for its sub-sites S3 through S1' under establishment of nine hydrophobic interactions, 14 hydrogen bonds and one salt bridge. In addition, an inhibitor carbonyl carbon that mimics the scissile carbonyl of substrates is pyramidalized and just 2.02 A away from the catalytic nucleophile of Kgp, C477Sgamma
the crystal structure of a domain within the haemagglutinin region of Kgp is reported here. The K2 domain structure is a jellyroll fold with two anti-parallel beta-sheets. This fold topology is shared with adhesive domains from functionally diverse receptors such as MAM domains, ephrin receptor ligand binding domains and a number of carbohydrate binding modules
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
construction of kgp-deficient mutant strains WS1, WS10, and WS15, and of Kgp and HmuR double mutants, which show reduced hemoglobin degradation and utilization due to abolished enzyme activity, Arg-specific gingipain R, EC 3.4.22.37, can compensate partially for the mutation, overview
additional information
-
construction of several C-terminally truncated enzyme mutant strains, which show decreased activity compared to the wild-type strain as well as altered distribution of the enzyme between membrane-associated and secreted forms, overview
additional information
-
kgp-deficient mutant strain WS10 shows 22 fold increased hmuR expression, while the kgp expression is decreased in the hmuR-deficient mutant strain WS1
additional information
-
complement killing resistancy of Porphyromonas gingivalis is examined using Arg- and Lys-gingipain (K1A) deletion mutants and polysaccharide synthesis deletion mutants. Arg- and Lys-gingipain (K1A) deletion mutants maintained resistance to killing
additional information
-
strains: Rgp/Kgp-null (rgpA rgpB kgpdeficient) triple-mutant KDP136 and the Kgp-null mutant (KDP129)
additional information
-
the results indicate that the Cys477 residue is essential for both the Kgp activity and the black pigmentation of Porphyromonas gingivalis
additional information
-
UV-visible spectroscopy is used to examine the interaction of iron(III) protoporphyrin IX monomers [Fe(III)PPIX.OH] with recombinant HA2 and purified HRgpA, Kgp and RgpB gingipains.The HA2 domain of Kgp reacts with Fe(III)PPIX.OH to form micro-oxo bishaem, the presence of which is confirmed by Fourier transform infrared spectroscopy. Both HRgpA and Kgp, but not RgpB, also mediate micro-oxo bishaem formation and aggregation
additional information
-
construction of a strain producing Kgp proteinase without the adhesin domains in a Rgp/Kgp/adhesin-null mutant, mutant strains 33277, KDP133, and KDP160 phenotypes, overview
additional information
-
construction of enzyme-deficient mutants KDP136 with DELTArgpADELTArgpBDELTAkgp, and KDP129 with DELTArgpADELTArgpB. The mutants do not, in contrast to the wild-type enzyme, inhibit cellular proliferation and don not arrest the cell cycle in the G0/G1 phase as well as decrease the expression levels of the cell-cycle regulatory molecules cyclin D and cyclin E in murine ST2 cells, overview
additional information
-
gingipain-deficient Porphyromonas gingivalis mutants lacking both Arg- and Lys-gingipains are unable to induce interleukin-1beta, interleukin-6, and interleukin-8 degradation
additional information
-
in the gene PG0027, encoding protein PG27, deletion mutant 83K10, the activities of Arg-gingipain and Lys-gingipain are severely reduced, while the activities of secreted exopeptidases DPPIV, DPP-7, and PTP-A are unaffected
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9
-
stable for several hours in the absence of cysteine, rapid loss of activity below pH 8.0 in the presence of cysteine
638843
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
60
45
-
68% loss of activity after 10 min, 97% loss of activity after 30 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Kgp shows a loss of only 1% and 8% of initial activity after 7 and 24 h, respectively
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Lys-gingipain is purified from the cell envelope extract of Porphyromonas gingivalis KDP112 by affinity chromatography on arginine Sepharose 4B
-
native Lys-gingipain from cell culture supernatant, re-activation of the proteases by reducing the active-centre thiol group partially oxidized during the purification process
-
purified by using gel-filtration and arginine-Sepharose chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant enzymes in murine ST2 osteoblastic/stromal cells
-
the gene fragment encoding the K2 domain (Ala1157-Gly1334) of Kgp from Porphyromonas gingivalis W83 is cloned into a modified vector pET-32a. The constructed plasmid is transformed into Escherichia coli BL21(DE3) competent cells for protein expression
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
molecular biology
medicine
-
development of structure-based inhibitors for treatment of periodontal diseases
medicine
-
results indicate that degradation of apoB-100 by Rgp but not Kgp plays a crucial role in the promotion of atherosclerosis by Porphyromonas gingivalis infection
medicine
-
development of potent, gingipain-specific inhibitors might be a helpful tool in a therapeutic strategy to prevent or treat periodontal disease
molecular biology
-
a combination of both R- and K-gingipains is required for pigment production from oxyhemoglobin by Porphyromonas gingivalis since R-gingipain converts oxyhemoglobin into the methemoglobin form which is more susceptible to Kgp degradation for the eventual release of iron(III) protoporphyrin IX and production of the micro-oxo haem dimer
molecular biology
-
it is shown that the production of anionic polysaccharide at the surface of Porphyromonas gingivalis rather than Arg- and Lys-gingipain synthesis is the principal mechanism of serum resistance in Porphyromonas gingivalis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Potempa, J.; Pike, R.; Travis, J.
The multiple forms of trypsin-like activity present in various strains of Porphyromonas gingivalis are due to the presence of either Arg-gingipain or Lys-gingipain
Infect. Immun.
63
1176-1182
1995
Porphyromonas gingivalis, Porphyromonas gingivalis H66
Bedi, G.S.
Purification and characterization of lysine- and arginine-specific gingivain proteases from Porphyromonas gingivalis
Prep. Biochem.
24
251-261
1994
Porphyromonas gingivalis
Pike, R.; McGraw, W.; Potempa, J.; Travis, J.
Lysine- and arginine-specific proteinases from Porphyromonas gingivalis. Isolation, characterization, and evidence for the existence of complexes with hemagglutinins
J. Biol. Chem.
269
406-411
1994
Porphyromonas gingivalis, Porphyromonas gingivalis H66
Potempa, J.; Travis, J.
Porphyromonas gingivalis proteinases in periodontitis, a review
Acta Biochim. Pol.
43
455-465
1996
Porphyromonas gingivalis
Pavloff, N.; Pemberton, P.A.; Potempa, J.; Chen, W.C.; Pike, R.N.; Prochazka, V.; Kiefer, M.C.; Travis, J.; Barr, P.J.
Molecular cloning and characterization of Porphyromonas gingivalis lysine-specific gingipain. A new member of an emerging family of pathogenic bacterial cysteine proteinases
J. Biol. Chem.
272
1595-1600
1997
Porphyromonas gingivalis (P72197), Porphyromonas gingivalis
Abe, N.; Kadowaki, T.; Okamoto, K.; Nakayama, K.; Ohishi, M.; Yamamoto, K.
Biochemical and functional properties of lysine-specific cysteine proteinase (Lys-gingipain) as a virulence factor of Porphyromonas gingivalis in periodontal disease
J. Biochem.
123
305-312
1998
Porphyromonas gingivalis
Fujimura, S.; Hirai, K.; Shibata, Y.; Nakayama, K.; Nakamura, T.
Comparative properties of envelope-associated arginine-gingipains and lysine-gingipain of Porphyromonas gingivalis
FEMS Microbiol. Lett.
163
173-179
1998
Porphyromonas gingivalis
Banbula, A.; Bugno, M.; Kuster, A.; Heinrich, P.C.; Travis, J.; Potempa, J.
Rapid and efficient inactivation of IL-6 gingipains, lysine- and arginine-specific proteinases from Porphyromonas Gingivalis
Biochem. Biophys. Res. Commun.
261
598-602
1999
Porphyromonas gingivalis
Sroka, A.; Sztukowska, M.; Potempa, J.; Travis, J.; Genco, C.A.
Degradation of host heme proteins by lysine- and arginine-specific cysteine proteinases (gingipains) of Porphyromonas gingivalis
J. Bacteriol.
183
5609-5616
2001
Porphyromonas gingivalis
Olczak, T.; Dixon, D.W.; Genco, C.A.
Binding specificity of the Porphyromonas gingivalis heme and hemoglobin receptor HmuR, gingipain K, and gingipain R1 for heme, porphyrins, and metalloporphyrins
J. Bacteriol.
183
5599-5608
2001
Porphyromonas gingivalis, Porphyromonas gingivalis HG66
Curtis, M.A.; Opoku, J.A.; Rangarajan, M.; Gallagher, A.; Sterne, J.A.C.; reid, C.R.; Evans, H.E.A.; Samuelsson, B.
Attenuation of the virulence of Porphyromonas gingivalis by using a specific synthetic Kgp protease inhibitor
Infect. Immun.
70
6968-6975
2002
Porphyromonas gingivalis
Nassar, H.; Chou, H.H.; Khlgatian, M.; Gibson, F.C., 3rd; Van Dyke, T.E.; Genco, C.A.
Role for fimbriae and lysine-specific cysteine proteinase gingipain K in expression of interleukin-8 and monocyte chemoattractant protein in Porphyromonas gingivalis-infected endothelial cells
Infect. Immun.
70
268-276
2002
Porphyromonas gingivalis
Baba, A.; Kadowaki, T.; Asao, T.; Yamamoto, K.
Roles for Arg- and Lys-gingipains in the disruption of cytokine responses and loss of viability of human endothelial cells by Porphyromonas gingivalis infection
Biol. Chem.
383
1223-1230
2002
Porphyromonas gingivalis
Simpsonv, W.; Olczak, T.; Genco, C.A.
Lysine-specific gingipain K and heme/hemoglobin receptor HmuR are involved in heme utilization in Porphyromonas gingivalis
Acta Biochim. Pol.
51
253-262
2004
Porphyromonas gingivalis
Smalley, J.W.; Thomas, M.F.; Birss, A.J.; Withnall, R.; Silver, J.
A combination of both arginine- and lysine-specific gingipain activity of Porphyromonas gingivalis is necessary for the generation of the micro-oxo bishaem-containing pigment from haemoglobin
Biochem. J.
379
833-840
2004
Porphyromonas gingivalis
Abe, N.; Baba, A.; Takii, R.; Nakayama, K.; Kamaguchi, A.; Shibata, Y.; Abiko, Y.; Okamoto, K.; Kadowaki, T.; Yamamoto, K.
Roles of Arg- and Lys-gingipains in coaggregation of Porphyromonas gingivalis: identification of its responsible molecules in translation products of rgpA, kgp, and hagA genes
Biol. Chem.
385
1041-1047
2004
Porphyromonas gingivalis
Liu, X.; Sroka, A.; Potempa, J.; Genco, C.A.
Coordinate expression of the Porphyromonas gingivalis lysine-specific gingipain proteinase, Kgp, arginine-specific gingipain proteinase, RgpA, and the heme/hemoglobin receptor, HmuR
Biol. Chem.
385
1049-1057
2004
Porphyromonas gingivalis
Mezyk-Kopec, R.; Bzowska, M.; Potempa, J.; Bzowska, M.; Jura, N.; Sroka, A.; Black, R.A.; Bereta, J.
Inactivation of membrane tumor necrosis factor alpha by gingipains from Porphyromonas gingivalis
Infect. Immun.
73
1506-1514
2005
Porphyromonas gingivalis
Bialas, A.; Grembecka, J.; Krowarsch, D.; Otlewski, J.; Potempa, J.; Mucha, A.
Exploring the Sn binding pockets in gingipains by newly developed inhibitors: structure-based design, chemistry, and activity
J. Med. Chem.
49
1744-1753
2006
Porphyromonas gingivalis, Porphyromonas gingivalis HG66
Kishimoto, M.; Yoshimura, A.; Naito, M.; Okamoto, K.; Yamamoto, K.; Golenbock, D.T.; Hara, Y.; Nakayama, K.
Gingipains inactivate a cell surface ligand on Porphyromonas gingivalis that induces TLR2-and TLR4-independent signaling
Microbiol. Immunol.
50
315-325
2006
Porphyromonas gingivalis
Sztukowska, M.; Sroka, A.; Bugno, M.; Banbula, A.; Takahashi, Y.; Pike, R.N.; Genco, C.A.; Travis, J.; Potempa, J.
The C-terminal domains of the gingipain K polyprotein are necessary for assembly of the active enzyme and expression of associated activities
Mol. Microbiol.
54
1393-1408
2004
Porphyromonas gingivalis
Cronan, C.A.; Potempa, J.; Travis, J.; Mayo, J.A.
Inhibition of Porphyromonas gingivalis proteinases (gingipains) by chlorhexidine: synergistic effect of Zn(II)
Oral Microbiol. Immunol.
21
212-217
2006
Porphyromonas gingivalis
Smalley, J.W.; Birss, A.J.; Szmigielski, B.; Potempa, J.
Sequential action of R- and K-specific gingipains of Porphyromonas gingivalis in the generation of the haem-containing pigment from oxyhemoglobin
Arch. Biochem. Biophys.
465
44-49
2007
Porphyromonas gingivalis
Ishida, Y.; Hu, J.; Sakai, E.; Kadowaki, T.; Yamamoto, K.; Tsukuba, T.; Kato, Y.; Nakayama, K.; Okamoto, K.
Determination of active site of lysine-specific cysteine proteinase (Lys-gingipain) by use of a Porphyromonas gingivalis plasmid system
Arch. Oral Biol.
56
538-544
2008
Porphyromonas gingivalis
Slaney, J.M.; Gallagher, A.; Aduse-Opoku, J.; Pell, K.; Curtis, M.A.
Mechanisms of resistance of Porphyromonas gingivalis to killing by serum complement
Infect. Immun.
74
5352-5361
2006
Porphyromonas gingivalis
Hashimoto, M.; Kadowaki, T.; Tsukuba, T.; Yamamoto, K.
Selective proteolysis of apolipoprotein B-100 by Arg-gingipain mediates atherosclerosis progression accelerated by bacterial exposure
J. Biochem.
140
713-723
2006
Porphyromonas gingivalis
Smalley, J.W.; Birss, A.J.; Szmigielski, B.; Potempa, J.
The HA2 haemagglutinin domain of the lysine-specific gingipain (Kgp) of Porphyromonas gingivalis promotes micro-oxo bishaem formation from monomeric iron(III) protoporphyrin IX
Microbiology
152
1839-1845
2006
Porphyromonas gingivalis
Yasuhara, R.; Miyamoto, Y.; Takami, M.; Imamura, T.; Potempa, J.; Yoshimura, K.; Kamijo, R.
Lysine-specific gingipain promotes lipopolysaccharide- and active-vitamin D3-induced osteoclast differentiation by degrading osteoprotegerin
Biochem. J.
419
159-166
2009
Porphyromonas gingivalis, Porphyromonas gingivalis HG66
Smalley, J.W.; Birss, A.J.; Szmigielski, B.; Potempa, J.
Mechanism of methaemoglobin breakdown by the lysine-specific gingipain of the periodontal pathogen Porphyromonas gingivalis
Biol. Chem.
389
1235-1238
2008
Porphyromonas gingivalis
Uehara, A.; Imamura, T.; Potempa, J.; Travis, J.; Takada, H.
Gingipains from Porphyromonas gingivalis synergistically induce the production of proinflammatory cytokines through protease-activated receptors with Toll-like receptor and NOD1/2 ligands in human monocytic cells
Cell. Microbiol.
10
1181-1189
2008
Porphyromonas gingivalis
Ishiguro, I.; Saiki, K.; Konishi, K.
PG27 is a novel membrane protein essential for a Porphyromonas gingivalis protease secretion system
FEMS Microbiol. Lett.
292
261-267
2009
Porphyromonas gingivalis, Porphyromonas gingivalis W83
Uehara, A.; Naito, M.; Imamura, T.; Potempa, J.; Travis, J.; Nakayama, K.; Takada, H.
Dual regulation of interleukin-8 production in human oral epithelial cells upon stimulation with gingipains from Porphyromonas gingivalis
J. Med. Microbiol.
57
500-507
2008
Porphyromonas gingivalis, Porphyromonas gingivalis HG66
Bania, J.; Kubiak, A.; Wojtachnio, K.; Polanowski, A.
Pancreatic secretory trypsin inhibitor acts as an effective inhibitor of cysteine proteinases gingipains from Porphyromonas gingivalis
J. Periodont. Res.
43
232-236
2008
Porphyromonas gingivalis
Kato, T.; Tsuda, T.; Inaba, H.; Kawai, S.; Okahashi, N.; Shibata, Y.; Abiko, Y.; Amano, A.
Porphyromonas gingivalis gingipains cause G(1) arrest in osteoblastic/stromal cells
Oral Microbiol. Immunol.
23
158-164
2008
Porphyromonas gingivalis, Porphyromonas gingivalis ATCC 33277
Stathopoulou, P.G.; Benakanakere, M.R.; Galicia, J.C.; Kinane, D.F.
The host cytokine response to Porphyromonas gingivalis is modified by gingipains
Oral Microbiol. Immunol.
24
11-17
2009
Porphyromonas gingivalis
Taiyoji, M.; Shitomi, Y.; Taniguchi, M.; Saitoh, E.; Ohtsubo, S.
Identification of proteinaceous inhibitors of a cysteine proteinase (an Arg-specific gingipain) from Porphyromonas gingivalis in rice grain, using targeted-proteomics approaches
J. Proteome Res.
8
5165-5174
2009
Porphyromonas gingivalis
Kantyka, T.; Latendorf, T.; Wiedow, O.; Bartels, J.; Glaeser, R.; Dubin, G.; Schroeder, J.M.; Potempa, J.; Meyer-Hoffert, U.
Elafin is specifically inactivated by RgpB from Porphyromonas gingivalis by distinct proteolytic cleavage
Biol. Chem.
390
1313-1320
2009
Porphyromonas gingivalis (B2RLK2)
Stathopoulou, P.; Galicia, J.; Benakanakere, M.; Garcia, C.; Potempa, J.; Kinane, D.
Porphyromonas gingivalis induce apoptosis in human gingival epithelial cells through a gingipain-dependent mechanism
BMC Microbiol.
9
107
2009
Porphyromonas gingivalis
Kuboniwa, M.; Amano, A.; Hashino, E.; Yamamoto, Y.; Inaba, H.; Hamada, N.; Nakayama, K.; Tribble, G.D.; Lamont, R.J.; Shizukuishi, S.
Distinct roles of long/short fimbriae and gingipains in homotypic biofilm development by Porphyromonas gingivalis
BMC Microbiol.
9
105
2009
Porphyromonas gingivalis
Saiki, K.; Konishi, K.
The role of Sov protein in the secretion of gingipain protease virulence factors of Porphyromonas gingivalis
FEMS Microbiol. Lett.
302
166-174
2010
Porphyromonas gingivalis
Haruyama, K.; Yoshimura, A.; Naito, M.; Kishimoto, M.; Shoji, M.; Abiko, Y.; Hara, Y.; Nakayama, K.
Identification of a gingipain-sensitive surface ligand of Porphyromonas gingivalis that induces Toll-like receptor 2- and 4-independent NF-kappaB activation in CHO cells
Infect. Immun.
77
4414-4420
2009
Porphyromonas gingivalis
Furuta, N.; Takeuchi, H.; Amano, A.
Entry of Porphyromonas gingivalis outer membrane vesicles into epithelial cells causes cellular functional impairment
Infect. Immun.
77
4761-4770
2009
Porphyromonas gingivalis
Nhien, N.T.; Huy, N.T.; Naito, M.; Oida, T.; Uyen, D.T.; Huang, M.; Kikuchi, M.; Harada, S.; Nakayama, K.; Hirayama, K.; Kamei, K.
Neutralization of toxic haem by Porphyromonas gingivalis haemoglobin receptor
J. Biochem.
147
317-325
2010
Porphyromonas gingivalis
Fitzpatrick, R.E.; Aprico, A.; Wijeyewickrema, L.C.; Pagel, C.N.; Wong, D.M.; Potempa, J.; Mackie, E.J.; Pike, R.N.
High molecular weight gingipains from Porphyromonas gingivalis induce cytokine responses from human macrophage-like cells via a nonproteolytic mechanism
J. Innate Immun.
1
109-117
2009
Porphyromonas gingivalis
Inomata, M.; Ishihara, Y.; Matsuyama, T.; Imamura, T.; Maruyama, I.; Noguchi, T.; Matsushita, K.
Degradation of vascular endothelial thrombomodulin by arginine- and lysine-specific cysteine proteases from Porphyromonas gingivalis
J. Periodontol.
80
1511-1517
2009
Porphyromonas gingivalis
Giacaman, R.A.; Asrani, A.C.; Ross, K.F.; Herzberg, M.C.
Cleavage of protease-activated receptors on an immortalized oral epithelial cell line by Porphyromonas gingivalis gingipains
Microbiology
155
3238-3246
2009
Porphyromonas gingivalis
Li, N.; Yun, P.; Nadkarni, M.; Ghadikolaee, N.; Nguyen, K.; Lee, M.; Hunter, N.; Collyer, C.
Structure determination and analysis of a haemolytic gingipain adhesin domain from Porphyromonas gingivalis
Mol. Microbiol.
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861-873
2010
Porphyromonas gingivalis
Mahtout, H.; Chandad, F.; Rojo, J.M.; Grenier, D.
Porphyromonas gingivalis mediates the shedding and proteolysis of complement regulatory protein CD46 expressed by oral epithelial cells
Oral Microbiol. Immunol.
24
396-400
2009
Porphyromonas gingivalis
Toh, E.C.; Dashper, S.G.; Huq, N.L.; Attard, T.J.; OBrien-Simpson, N.M.; Chen, Y.Y.; Cross, K.J.; Stanton, D.P.; Paolini, R.A.; Reynolds, E.C.
Porphyromonas gingivalis cysteine proteinase inhibition by kappa-casein peptides
Antimicrob. Agents Chemother.
55
1155-1161
2011
Porphyromonas gingivalis
Dashper, S.G.; Pan, Y.; Veith, P.D.; Chen, Y.Y.; Toh, E.C.; Liu, S.W.; Cross, K.J.; Reynolds, E.C.
Lactoferrin inhibits Porphyromonas gingivalis proteinases and has sustained biofilm inhibitory activity
Antimicrob. Agents Chemother.
56
1548-1556
2012
Porphyromonas gingivalis
Vincents, B.; Guentsch, A.; Kostolowska, D.; von Pawel-Rammingen, U.; Eick, S.; Potempa, J.; Abrahamson, M.
Cleavage of IgG1 and IgG3 by gingipain K from Porphyromonas gingivalis may compromise host defense in progressive periodontitis
FASEB J.
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3741-3750
2011
Porphyromonas gingivalis
Maisetta, G.; Brancatisano, F.; Esin, S.; Campa, M.; Batoni, G.
Gingipains produced by Porphyromonas gingivalis ATCC49417 degrade human-beta-defensin 3 and affect peptides antibacterial activity in vitro
Peptides
32
1073-1077
2011
Porphyromonas gingivalis
Smalley, J.; Byrne, D.; Birss, A.; Wojtowicz, H.; Sroka, A.; Potempa, J.; Olczak, T.
HmuY haemophore and gingipain proteases constitute a unique syntrophic system of haem acquisition by Porphyromonas gingivalis
PLoS ONE
6
e17182
2011
Porphyromonas gingivalis
Pomowski, A.; Uson, I.; Nowakowska, Z.; Veillard, F.; Sztukowska, M.N.; Guevara, T.; Goulas, T.; Mizgalska, D.; Nowak, M.; Potempa, B.; Huntington, J.A.; Potempa, J.; Gomis-Rueth, F.X.
Structural insights unravel the zymogenic mechanism of the virulence factor gingipain K from Porphyromonas gingivalis, a causative agent of gum disease from the human oral microbiome
J. Biol. Chem.
292
5724-5735
2017
Porphyromonas gingivalis (Q51817), Porphyromonas gingivalis, Porphyromonas gingivalis W83 (Q51817)
Guevara, T.; Rodriguez-Banqueri, A.; Lasica, A.M.; Ksiazek, M.; Potempa, B.A.; Potempa, J.; Gomis-Rueth, F.X.
Structural determinants of inhibition of Porphyromonas gingivalis gingipain K by KYT-36, a potent, selective, and bioavailable peptidase inhibitor
Sci. Rep.
9
4935
2019
Porphyromonas gingivalis (Q51817), Porphyromonas gingivalis, Porphyromonas gingivalis W83 (Q51817)
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