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alpha chains of haptoglobin + H2O
?
alpha-globin + H2O
?
-
absolutely specific cleavage of all Arg-Xaa peptides bonds, in presence of 4 M urea, because alpha-globin is not soluble at neutral pH
-
?
alpha-thrombin + H2O
beta-thrombin B-1 and B-2 chains
-
HRgpA and RgpB, cleavage of peptide bond R383-N394
-
?
alpha1-Antichymotrypsin + H2O
?
apoB-100 protein + H2O
?
-
apoB-100 degradation induces LDL-modification and contributes to the onset of atherosclerosis
-
-
?
AWTPTPTPLSTPSIIRTTGLRPYPSSVLI + H2O
AWTPTPTPLSTPSIIR + TTGLRPYPSSVLI
benzoyl-Arg 4-nitroanilide + H2O
benzoyl-Arg + 4-nitroaniline
-
-
-
-
?
benzoyl-Arg-4-nitroanilide + H2O
benzoyl-Arg + 4-nitroaniline
-
-
-
-
?
Benzoyl-Ile-Glu-(gamma-ornithyl)-Gly-Arg 4-nitroanilide + H2O
?
-
-
-
-
?
benzoyl-L-arginine-4-nitroanilide + H2O
benzoyl-L-arginine + 4-nitroaniline
benzoyl-Phe-Val-Arg-4-nitroanilide + H2O
benzoyl-Phe-Val-Arg + 4-nitroaniline
-
-
-
?
benzoyl-Pro-Phe-Arg-4-nitroanilide + H2O
benzoyl-Pro-Phe-Arg + 4-nitroaniline
-
-
-
?
benzoyl-Val-Gly-Arg-4-nitroanilide + H2O
benzoyl-Val-Gly-Arg + 4-nitroaniline
-
-
-
?
beta-globin + H2O
?
-
absolutely specific cleavage of all Arg-Xaa peptides bonds, in presence of 4 M urea, because beta-globin is not soluble at neutral pH
-
?
beta-thrombin B-2 chain + H2O
?
-
HRgpA and RgpB, substrate inactivation and degradation
-
?
butoxy-carbonyl-O-benzyl-Ser-Gly-Arg-4-nitroanilide + H2O
butoxy-carbonyl-O-benzyl-Ser-Gly-Arg + 4-nitroaniline
-
best sythetic substrate
-
?
butoxy-carbonyl-Val-Leu-Gly-Arg-4-nitroanilide + H2O
butoxy-carbonyl-Val-Leu-Gly-Arg + 4-nitroaniline
-
-
-
?
Bz-L-Arg-4-nitroanilide + H2O
Bz-L-Arg + 4-nitroaniline
-
-
-
-
?
C3 protein + H2O
?
-
-
-
-
?
C4 protein + H2O
?
-
-
-
-
?
C5 protein + H2O
?
-
at higher enzyme concentrations
-
-
?
CBZ-Phe-Arg-4-methyl-coumaryl-7-amide + H2O
CBZ-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
CD27 protein + H2O
?
-
involved in reduction of T-cell function, effective even in the presence of 2.5 or 5% serum
-
-
?
cell adhesion molecule + H2O
?
-
involved in the detachment of endothelial cells
-
-
?
D-Ile-Pro-Arg 4-nitroanilide + H2O
?
-
-
-
-
?
D-Phe-Pip-Arg 4-nitroanilide + H2O
?
-
-
-
-
?
denatured alpha1-proteinase inhibitor + H2O
?
-
-
?
denatured type I collagen + H2O
?
factor IX proenzyme + H2O
?
-
activation through limited proteolysis
-
-
?
factor X proenzyme + H2O
?
-
activation through limited proteolysis
-
-
?
fibrinogen A alpha-chain + H2O
28 kDa fragment + ?
-
major cleavage site at position 22, all isoforms
the 28 kDa fragment is the major product of isoform HRgpA
?
fibrinogen B beta-chain + H2O
?
-
high activity of isoform HRgpA, which performs cleavage at 2 positions: 42 and 44
-
?
Fibronectin + H2O
?
-
the enzyme isoforms HRgpA and RgpB effectively destroy the cell-binding domain of fibronectin
-
-
?
Glycophorin A + H2O
?
-
-
-
-
?
haemoglobin + H2O
?
-
complete digestion, enzyme form RGP-B shows high activity, not RGP-A, human substrate
-
?
haptoglobin + H2O
?
-
degradation of host protein substrate
-
-
?
Hemoglobin + H2O
?
-
degradation of host protein substrate
-
-
?
hemopexin + H2O
?
-
degradation of host protein substrate
-
-
?
hemopexin + H2O
hemin + ?
human beta-defensin 3 + H2O
?
-
-
-
-
?
human protease-activated receptor PAR-1 + H2O
?
human protease-activated receptor PAR-2 + H2O
?
Insulin B-chain + H2O
?
-
specific cleavage of Arg-+-
-
-
?
integrin subunit alpha2 + H2O
?
integrin subunit beta1 + H2O
?
integrin subunit beta3 + H2O
?
interleukin-1beta + H2O
?
Leu-Tyr-Arg-4-nitroanilide + H2O
Leu-Tyr-Arg + 4-nitroaniline
synthetic fluorogenic substrate
-
?
Lysozyme + H2O
?
-
absolutely specific cleavage of all Arg-Xaa peptides bonds
-
?
Mellitin + H2O
?
-
specific cleavage of Arg-+-
-
-
?
MeoSuc-Ala-Ala-Pro-Val-4-nitroanilide + H2O
?
-
-
-
?
N-alpha-benzoyl-D,L-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + 4-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-DL-Arg-4-nitroanilide + H2O
N-alpha-benzoyl-DL-Arg + 4-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-DL-arginine 4-nitroanilide + H2O
N-alpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-DL-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-DL-arginine + 4-nitroaniline
N-alpha-benzoyl-DL-Lys-4-nitroanilide + H2O
N-alpha-benzoyl-DL-Lys + 4-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-L-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + 4-nitroaniline
-
-
-
-
?
N-benzoyl-L-arginine-4-nitroanilide + H2O
N-benzoyl-L-arginine + 4-nitroaniline
-
-
-
?
N-cadherin + H2O
?
-
in BCAEC cells, cleavage by HRgpA but not RgpB
-
-
?
N-p-tosyl-Gly-Pro-Arg-4-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Arg + 4-nitroaniline
Nalpha-benzoyl-D,L-Arg-4-nitroanilide + H2O
Nalpha-benzoyl-D,L-Arg + 4-nitroaniline
-
-
-
-
?
Nalpha-benzoyl-D,L-arginine 4 nitroanilide + H2O
Nalpha-benzoyl-D,L-arginine + 4 nitroaniline
-
-
-
-
?
Nalpha-benzoyl-L-Arg-4-nitroanilide + H2O
Nalpha-benzoyl-L-Arg + 4-nitroanilide
-
-
-
-
?
Nalpha-benzoyl-L-Arg-4-nitroanilide + H2O
Nalpha-benzoyl-L-Arg + 4-nitroaniline
-
-
-
-
?
Nalpha-benzoyl-L-Arg-4-nitroanilide + H2O
Nalpha-benzoyl-L-Arg-4-nitroaniline
-
-
-
-
?
Nalpha-benzoyl-L-arginine 4-nitroanilide + H2O
Nalpha-benzoyl-L-arginine + 4-nitroaniline
oxyhaemoglobin + H2O
?
-
-
-
-
?
oxyhaemoglobin + H2O
methaemoglobin
oxyhaemoglobin + H2O
methaemoglobin + ?
prefimbrillin + H2O
fimbrilline + ?
-
-
mature form of the protein
-
?
profibronectin + H2O
fibronectin + ?
protease-activated receptor-1 + H2O
?
-
specific substrate for Arg-gingipain
-
-
?
protein C + H2O
?
-
activation through limited proteolysis
-
-
?
prothrombin + H2O
?
-
activation through limited proteolysis
-
-
?
prothrombin + H2O
alpha-thrombin + 2 peptide fragments
-
major cleavage sites of HRgpA are R271-T272, R320-I321, and R155-S156, activation of human substrate, HRgpA possesses adhesion domains and is about 20fold more active than the single chain RgpB
high amount od alpha-thrombin
?
prothrombin + H2O
alpha-thrombin + prethrombin 1 + prethrombin 2 + 1 peptide fragments
-
major cleavage sites of RgpB are R155-S156 and R271-T272, while the peptide bond R320-I321 is not efficiently cleaved resulting in about 20fold slower reaction, activation of human substrate, less active than HRgpA
low amount of alpha-thrombin
?
prothrombin + H2O
thrombin + ?
-
HRgpA, involved in fibrinogen clotting
-
?
RgpA-HagA polyprotein + H2O
?
-
processing of the precursor by Rgp
-
-
?
RgpA-Hgp polyprotein + H2O
?
ribonuclease A + H2O
?
-
absolutely specific cleavage of all Arg-Xaa peptides bonds
-
?
secretory leucocyte protease inhibitor + H2O
?
t-butyloxycarbonyl-L-leucylglycyl-L-arginine-4-metylcoumaryl-7-amide + H2O
?
-
-
-
-
?
thrombomodulin + H2O
?
-
Lys-gingipain and Arg-gingipain cleave thrombomodulin in vitro
-
-
?
toluenesulfonyl-glycyl-L-prolyl-L-arginine-4-nitroanilide + H2O
toluenesulfonyl-glycyl-L-prolyl-L-arginine + 4-nitroaniline
-
-
-
?
tosyl-Gly-L-Pro-L-Arg 4-nitroanilide + H2O
tosyl-Gly-L-Pro-L-Arg 4-nitroaniline
-
-
-
-
?
tosyl-GPR-4-nitroanilide + H2O
tosyl-GPR + 4-nitroaniline
other substrates with a Ps proline are very poor substrates, synthetic fluorogenic substrate
-
?
transferrin + H2O
?
-
degradation of host protein substrate
-
-
?
transferrin + H2O
hemin + ?
transferring receptor + H2O
?
-
Rgp is responsible for transferring receptor degradation
-
-
?
VE-cadherin + H2O
?
-
in BCAEC cells, especially HRgpA
-
-
?
Z-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg + 7-amino-4-methylcoumarin
Z-Arg-Arg-4-nitroanilide + H2O
Z-Arg-Arg + 4-nitroaniline
synthetic fluorogenic substrate
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
additional information
?
-
alpha chains of haptoglobin + H2O

?
-
low activity, hemoglobin protects
-
?
alpha chains of haptoglobin + H2O
?
-
low activity, hemoglobin protects
-
?
alpha1-Antichymotrypsin + H2O

?
inactivation of the substrate
-
?
alpha1-Antichymotrypsin + H2O
?
inactivation of the substrate
-
?
AWTPTPTPLSTPSIIRTTGLRPYPSSVLI + H2O

AWTPTPTPLSTPSIIR + TTGLRPYPSSVLI
-
-
-
-
?
AWTPTPTPLSTPSIIRTTGLRPYPSSVLI + H2O
AWTPTPTPLSTPSIIR + TTGLRPYPSSVLI
-
-
-
-
?
azocasein + H2O

?
-
-
-
?
azocasein + H2O
?
synthetic chromogenic substrate
-
?
azocasein + H2O
?
synthetic chromogenic substrate
-
?
Azocoll + H2O

?
-
-
-
-
?
Azocoll + H2O
?
-
-
-
-
?
benzoyl-L-arginine-4-nitroanilide + H2O

benzoyl-L-arginine + 4-nitroaniline
-
-
-
?
benzoyl-L-arginine-4-nitroanilide + H2O
benzoyl-L-arginine + 4-nitroaniline
-
-
-
-
?
benzoyl-L-arginine-4-nitroanilide + H2O
benzoyl-L-arginine + 4-nitroaniline
synthetic fluorogenic substrate
-
?
Collagen type I + H2O

?
-
not the purified isoforms, enzyme probably needs to be attached to the cell surface
-
?
Collagen type I + H2O
?
-
not the purified isoforms, enzyme probably needs to be attached to the cell surface
-
?
CXCL8 + H2O

?
-
-
-
-
?
denatured type I collagen + H2O

?
-
-
?
denatured type I collagen + H2O
?
-
-
?
elafin + H2O

?
all three gingipains have the ability to degrade elafin (endogenous inhibitor secreted by epithelial cells)
-
-
?
elafin + H2O
?
all three gingipains have the ability to degrade elafin (endogenous inhibitor secreted by epithelial cells) with RgpB being far more efficient than other gingipains. RgpB efficiently inactivates the inhibitory activity of elafin at subnanomolar concentrations through proteolysis limited to the Arg22-Cys23 peptide bond within the surface loop harboring the inhibitor active site
-
-
?
Gelatin + H2O

?
-
purified isozymes
-
?
Gelatin + H2O
?
-
purified isozymes
-
?
hemopexin + H2O

hemin + ?
-
-
products of 23 kDa and 47 kDa, products of 23 kDa and 40 kDa in serum
?
hemopexin + H2O
hemin + ?
-
-
products of 23 kDa and 47 kDa, products of 23 kDa and 40 kDa in serum
?
histatin 5 + H2O

?
-
-
-
-
?
histatin 5 + H2O
?
-
-
-
-
?
human protease-activated receptor PAR-1 + H2O

?
-
-
-
-
?
human protease-activated receptor PAR-1 + H2O
?
-
PAR-1 activation on epithelial cells
-
-
?
human protease-activated receptor PAR-1 + H2O
?
-
-
-
-
?
human protease-activated receptor PAR-1 + H2O
?
-
PAR-1 activation on epithelial cells
-
-
?
human protease-activated receptor PAR-2 + H2O

?
-
-
-
-
?
human protease-activated receptor PAR-2 + H2O
?
-
PAR-2 activation on epithelial cells
-
-
?
human protease-activated receptor PAR-2 + H2O
?
-
-
-
-
?
integrin subunit alpha2 + H2O

?
-
-
-
?
integrin subunit alpha2 + H2O
?
-
-
-
?
integrin subunit beta1 + H2O

?
-
-
-
?
integrin subunit beta1 + H2O
?
-
-
-
?
integrin subunit beta3 + H2O

?
-
-
-
?
integrin subunit beta3 + H2O
?
-
-
-
?
interferon gamma + H2O

?
-
degradation
-
-
?
interferon gamma + H2O
?
-
degradation leading to local cytokine paralysis impairing the inflammation-dependent host defense mechanisms
-
-
?
interleukin 12 + H2O

?
-
degradation
-
-
?
interleukin 12 + H2O
?
-
degradation leading to local cytokine paralysis impairing the inflammation-dependent host defense mechanisms
-
-
?
interleukin-1beta + H2O

?
-
low activity
-
-
?
interleukin-1beta + H2O
?
-
biological inactivation and degradation, low activity, cytokine degradation is mainly the result of Lys-gingipain, EC 3.4.22.47
-
-
?
interleukin-6 + H2O

?
-
-
-
-
?
interleukin-6 + H2O
?
-
biological inactivation and degradation
-
-
?
interleukin-8 + H2O

?
-
-
-
-
?
interleukin-8 + H2O
?
-
biological inactivation and degradation
-
-
?
Muc2 + H2O

?
-
-
-
-
?
N-alpha-benzoyl-DL-arginine-4-nitroanilide + H2O

N-alpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-DL-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
?
N-alpha-benzoyl-DL-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-DL-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
?
N-alpha-benzoyl-DL-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-DL-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
?
N-p-tosyl-Gly-Pro-Arg-4-nitroanilide + H2O

N-p-tosyl-Gly-Pro-Arg + 4-nitroaniline
-
-
-
-
?
N-p-tosyl-Gly-Pro-Arg-4-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Arg + 4-nitroaniline
-
-
-
-
?
Nalpha-benzoyl-L-arginine 4-nitroanilide + H2O

Nalpha-benzoyl-L-arginine + 4-nitroaniline
-
-
-
-
?
Nalpha-benzoyl-L-arginine 4-nitroanilide + H2O
Nalpha-benzoyl-L-arginine + 4-nitroaniline
-
-
-
-
?
oxyhaemoglobin + H2O

methaemoglobin
-
data indicate direct product formation without the occurrence of intermediates, reaction required for the formation the the my-oxo heam dimer containing black pigment
-
-
?
oxyhaemoglobin + H2O
methaemoglobin
-
data indicate direct product formation without the occurrence of intermediates, reaction required for the formation the the my-oxo heam dimer containing black pigment
-
-
?
oxyhaemoglobin + H2O

methaemoglobin + ?
-
data indicate direct product formation without the occurrence of intermediates
-
-
?
oxyhaemoglobin + H2O
methaemoglobin + ?
-
data indicate direct product formation without the occurrence of intermediates
-
-
?
profibronectin + H2O

fibronectin + ?
-
-
-
?
profibronectin + H2O
fibronectin + ?
-
-
-
?
protein + H2O

peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
?
RgpA-Hgp polyprotein + H2O

?
-
processing of the precursor by Rgp
-
-
?
RgpA-Hgp polyprotein + H2O
?
-
processing of the precursor by Rgp, Porphyromonas gingivalis-induced platelet aggregation in platelet-rich plasma depends on processed Hgp44 adhesin but not directly on Rgp proteinase, the adhesin is also processed by Lys-gingipain Kgp, EC 3.4.22.47
-
-
?
secretory leucocyte protease inhibitor + H2O

?
-
reduction of the protective effect of SLPIon neutrophil proteases and bacterial proinflammatory compounds
-
-
?
secretory leucocyte protease inhibitor + H2O
?
-
recombinant protein, reaction catalyzed by RgpA and RgpB
-
-
?
TNFalpha + H2O

?
-
degradation
-
-
?
TNFalpha + H2O
?
-
degradation leading to local cytokine paralysis impairing the inflammation-dependent host defense mechanisms
-
-
?
TNFalpha + H2O
?
-
inactivation by degradation of human TNFalpha on host cell surface and recombinant fibroblast cell surface, leading to inhibition of biological functions of TNFalpha, overview
-
-
?
TNFalpha + H2O
?
-
degradation, high activity with HRgpA, moderate activity with RgpB
-
-
?
transferrin + H2O

hemin + ?
-
-
-
?
transferrin + H2O
hemin + ?
-
slight truncation of the polypeptide chain in serum
-
?
transferrin + H2O
hemin + ?
-
-
-
?
transferrin + H2O
hemin + ?
-
slight truncation of the polypeptide chain in serum
-
?
Z-Arg-7-amido-4-methylcoumarin + H2O

Z-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O

Z-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
additional information

?
-
-
hydrolysis of synthetic chromogenic substrates with arginine in the P1 position
-
-
?
additional information
?
-
-
no activity of both enzyme forms with toluenesulfonyl-glycyl-L-prolyl-L-lysine-4-nitroanilide, Val-Leu-Lys-4-nitroanilide, benzoyl-Lys-4-nitroanilide, succinyl-Ala-Ala-Pro-Phe-4-nitroanilide, glutaryl-Phe-4-nitroanilide, benzoyl-Tyr-4-nitroanilide, and Lys-4-nitroanilide, activity with chromogenic synthetic substrates is limited to those with arginine in the P1-position
-
?
additional information
?
-
-
substrate specificity for the C-terminal position next to the cleavage site of the different enzyme forms, overview
-
?
additional information
?
-
-
substrate specificity, no inactivation of native alpha1-proteinase inhibitor and native type I collagen
-
?
additional information
?
-
substrate specificity, no inactivation of native alpha1-proteinase inhibitor and native type I collagen
-
?
additional information
?
-
substrate specificity, no inactivation of native alpha1-proteinase inhibitor and native type I collagen
-
?
additional information
?
-
-
the enzyme makes a significant contribution to the virulence of Porphyromonas gingivalis
-
-
?
additional information
?
-
-
enzyme disrupts interaction between fibronectin and integrin in human fibroblasts, leading to cell death of detached fibroblasts, which contributes to the tissue damage in periodontal disease caused by Porphyromonas gingivalis
-
?
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
?
-
-
gingipains are essential for bacterial virulence and survival
-
-
?
additional information
?
-
-
gingipains cleave a broad range of in-host proteins and are key virulence factors in the onset and development of human adult periodontitis, the enzyme stimulates production of hepatocyte growth factor, i.e. scatter factor, through protease-activated receptors in human gingival fibroblasts in culture, overview
-
-
?
additional information
?
-
-
gingipains R are potent permeability enhancement factors by prekallikrein activation and bradykinin induction, the enzyme degrades proteins of connective tissue, cell surface proteins and receptors, cytokines and plasma proteins, including components of the coagulation and complement cascades, heme- and iron-binding proteins, immunoglobulins and proteinase inhibitors
-
-
?
additional information
?
-
-
gingipains R mediate coaggregation of Porphyromonas gingivalis with other bacteria, overview
-
-
?
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
-
-
?
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
?
-
-
gingipains are cysteine proteinases
-
-
?
additional information
?
-
-
gingipains are cysteine proteinases cleaving a broad range of in-host proteins
-
-
?
additional information
?
-
-
role of the Sn binding pocket, molecular basis for substrate specificity, overview
-
-
?
additional information
?
-
-
the enzyme is specific for peptide substrate with Arg at P1 position, gingipain R performs autoprocessing and activation
-
-
?
additional information
?
-
-
implicated in a wide range of both pathological and physiological processes of Porphyromonas gingivalis, including destruction of periodontal tissue, disruption of host defense mechanisms, processing of bacterial cell surface and secretory proteins, and acquisition of heme and amino acids, involved in atherosclerotic processes
-
-
?
additional information
?
-
-
important for the provision of nutrients for the bacterium in the host organism, destruction of host tissue, modulation of host immune response
-
-
?
additional information
?
-
-
important virulence factors in periodontitis
-
-
?
additional information
?
-
-
important virulence factors in periodontitis
-
-
?
additional information
?
-
-
important virulence factors in periodontitis
-
-
?
additional information
?
-
-
important virulence factors in periodontitis
-
-
?
additional information
?
-
-
important virulence factors in periodontitis
-
-
?
additional information
?
-
-
important virulence factors in periodontitis, activation of the C1 complex in serum, degradation of multiple complement components, important factor for the resistance to the bacteriolytic activity of serum
-
-
?
additional information
?
-
-
important virulence factors in periodontitis, involved in the perturbation of host defense and the destruction and invasion of host tissues, degradation of hostâs proteins such as ICAM-1m VCAM-1, catenins, and cadherins, involved in the shedding of syndecan-1
-
-
?
additional information
?
-
-
important virulence factors in periodontitis, probably involved in the reduction of T-cell function at periodontal lesion sites, induction of PAR-1 and PAR-2 receptor expression, up-regulation of PAR-4 expression, little effect on PAR-3 expression, increases expression of CD69 and CD25 on T-cells
-
-
?
additional information
?
-
-
involved in the deregulation of the hostâs inflammatory response
-
-
?
additional information
?
-
-
involved in the induction of apoptosis in caspase dependent and caspase independent pathway
-
-
?
additional information
?
-
-
involved in the regulation of mRNA expression for the receptor activator of NF-kappaB ligand (RANKL) protein
-
-
?
additional information
?
-
-
no degradation of ICAM-3
-
-
?
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 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, overview
-
-
?
additional information
?
-
-
gingipains are involved in bacterial adherence to host cells, RgpA binds to adhesin via its adhesin binding domain. Peptide A44 derived from the adhesin domain of RgpA plays a role in binding of Porphyromonas gingivalis to HEP-2 epithelial cells via cell surface receptors, e.g. clathrin, nocodazole and paclitaxel, which disrupt microtubule formation, block the interaction, while genistein does not
-
-
?
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
?
-
-
HRgpA-mediated downregulation and RgpB-mediated upregulation of production of interleukin-8, occurs through protease-activated receptors, PAR-1 and PAR-2, signalling, RgpB-mediated upregulation of IL-8 production occurs through nuclear factor-kappa B, which does not affect HRgpA-mediated downregulation, overview. Gingipains preferentially suppress IL-8, resulting in attenuation of the cellular recognition of bacteria, and as a consequence, sustain chronic inflammation
-
-
?
additional information
?
-
-
RgpA and RgpB cleave proteins after arginine residues
-
-
?
additional information
?
-
-
enzyme disrupts interaction between fibronectin and integrin in human fibroblasts, leading to cell death of detached fibroblasts, which contributes to the tissue damage in periodontal disease caused by Porphyromonas gingivalis
-
?
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
?
-
-
gingipains cleave a broad range of in-host proteins and are key virulence factors in the onset and development of human adult periodontitis, the enzyme stimulates production of hepatocyte growth factor, i.e. scatter factor, through protease-activated receptors in human gingival fibroblasts in culture, overview
-
-
?
additional information
?
-
-
gingipains are cysteine proteinases cleaving a broad range of in-host proteins
-
-
?
additional information
?
-
-
gingipains are essential for bacterial virulence and survival
-
-
?
additional information
?
-
-
role of the Sn binding pocket, molecular basis for substrate specificity, overview
-
-
?
additional information
?
-
-
HRgpA-mediated downregulation and RgpB-mediated upregulation of production of interleukin-8, occurs through protease-activated receptors, PAR-1 and PAR-2, signalling, RgpB-mediated upregulation of IL-8 production occurs through nuclear factor-kappa B, which does not affect HRgpA-mediated downregulation, overview. Gingipains preferentially suppress IL-8, resulting in attenuation of the cellular recognition of bacteria, and as a consequence, sustain chronic inflammation
-
-
?
additional information
?
-
-
substrate specificity, no inactivation of native alpha1-proteinase inhibitor and native type I collagen
-
?
additional information
?
-
substrate specificity, no inactivation of native alpha1-proteinase inhibitor and native type I collagen
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
apoB-100 protein + H2O
?
-
apoB-100 degradation induces LDL-modification and contributes to the onset of atherosclerosis
-
-
?
C3 protein + H2O
?
-
-
-
-
?
C4 protein + H2O
?
-
-
-
-
?
C5 protein + H2O
?
-
at higher enzyme concentrations
-
-
?
CD27 protein + H2O
?
-
involved in reduction of T-cell function, effective even in the presence of 2.5 or 5% serum
-
-
?
cell adhesion molecule + H2O
?
-
involved in the detachment of endothelial cells
-
-
?
factor IX proenzyme + H2O
?
-
activation through limited proteolysis
-
-
?
factor X proenzyme + H2O
?
-
activation through limited proteolysis
-
-
?
Fibronectin + H2O
?
-
the enzyme isoforms HRgpA and RgpB effectively destroy the cell-binding domain of fibronectin
-
-
?
Glycophorin A + H2O
?
-
-
-
-
?
haptoglobin + H2O
?
-
degradation of host protein substrate
-
-
?
Hemoglobin + H2O
?
-
degradation of host protein substrate
-
-
?
hemopexin + H2O
?
-
degradation of host protein substrate
-
-
?
hemopexin + H2O
hemin + ?
human protease-activated receptor PAR-1 + H2O
?
human protease-activated receptor PAR-2 + H2O
?
-
PAR-2 activation on epithelial cells
-
-
?
integrin subunit alpha2 + H2O
?
integrin subunit beta1 + H2O
?
integrin subunit beta3 + H2O
?
interferon gamma + H2O
?
-
degradation leading to local cytokine paralysis impairing the inflammation-dependent host defense mechanisms
-
-
?
interleukin 12 + H2O
?
-
degradation leading to local cytokine paralysis impairing the inflammation-dependent host defense mechanisms
-
-
?
interleukin-1beta + H2O
?
-
biological inactivation and degradation, low activity, cytokine degradation is mainly the result of Lys-gingipain, EC 3.4.22.47
-
-
?
interleukin-6 + H2O
?
-
biological inactivation and degradation
-
-
?
interleukin-8 + H2O
?
-
biological inactivation and degradation
-
-
?
oxyhaemoglobin + H2O
methaemoglobin
prefimbrillin + H2O
fimbrilline + ?
-
-
mature form of the protein
-
?
profibronectin + H2O
fibronectin + ?
protease-activated receptor-1 + H2O
?
-
specific substrate for Arg-gingipain
-
-
?
protein C + H2O
?
-
activation through limited proteolysis
-
-
?
prothrombin + H2O
?
-
activation through limited proteolysis
-
-
?
prothrombin + H2O
thrombin + ?
-
HRgpA, involved in fibrinogen clotting
-
?
RgpA-HagA polyprotein + H2O
?
-
processing of the precursor by Rgp
-
-
?
RgpA-Hgp polyprotein + H2O
?
-
processing of the precursor by Rgp, Porphyromonas gingivalis-induced platelet aggregation in platelet-rich plasma depends on processed Hgp44 adhesin but not directly on Rgp proteinase, the adhesin is also processed by Lys-gingipain Kgp, EC 3.4.22.47
-
-
?
secretory leucocyte protease inhibitor + H2O
?
-
reduction of the protective effect of SLPIon neutrophil proteases and bacterial proinflammatory compounds
-
-
?
transferrin + H2O
?
-
degradation of host protein substrate
-
-
?
transferrin + H2O
hemin + ?
transferring receptor + H2O
?
-
Rgp is responsible for transferring receptor degradation
-
-
?
additional information
?
-
Collagen type I + H2O

?
-
not the purified isoforms, enzyme probably needs to be attached to the cell surface
-
?
Collagen type I + H2O
?
-
not the purified isoforms, enzyme probably needs to be attached to the cell surface
-
?
CXCL8 + H2O

?
-
-
-
-
?
elafin + H2O

?
all three gingipains have the ability to degrade elafin (endogenous inhibitor secreted by epithelial cells)
-
-
?
elafin + H2O
?
all three gingipains have the ability to degrade elafin (endogenous inhibitor secreted by epithelial cells) with RgpB being far more efficient than other gingipains. RgpB efficiently inactivates the inhibitory activity of elafin at subnanomolar concentrations through proteolysis limited to the Arg22-Cys23 peptide bond within the surface loop harboring the inhibitor active site
-
-
?
hemopexin + H2O

hemin + ?
-
-
products of 23 kDa and 40 kDa in serum
?
hemopexin + H2O
hemin + ?
-
-
products of 23 kDa and 40 kDa in serum
?
histatin 5 + H2O

?
-
-
-
-
?
histatin 5 + H2O
?
-
-
-
-
?
human protease-activated receptor PAR-1 + H2O

?
-
PAR-1 activation on epithelial cells
-
-
?
human protease-activated receptor PAR-1 + H2O
?
-
PAR-1 activation on epithelial cells
-
-
?
integrin subunit alpha2 + H2O

?
-
-
-
?
integrin subunit alpha2 + H2O
?
-
-
-
?
integrin subunit beta1 + H2O

?
-
-
-
?
integrin subunit beta1 + H2O
?
-
-
-
?
integrin subunit beta3 + H2O

?
-
-
-
?
integrin subunit beta3 + H2O
?
-
-
-
?
Muc2 + H2O

?
-
-
-
-
?
oxyhaemoglobin + H2O

methaemoglobin
-
data indicate direct product formation without the occurrence of intermediates, reaction required for the formation the the my-oxo heam dimer containing black pigment
-
-
?
oxyhaemoglobin + H2O
methaemoglobin
-
data indicate direct product formation without the occurrence of intermediates, reaction required for the formation the the my-oxo heam dimer containing black pigment
-
-
?
profibronectin + H2O

fibronectin + ?
-
-
-
?
profibronectin + H2O
fibronectin + ?
-
-
-
?
protein + H2O

peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
?
TNFalpha + H2O

?
-
degradation leading to local cytokine paralysis impairing the inflammation-dependent host defense mechanisms
-
-
?
TNFalpha + H2O
?
-
inactivation by degradation of human TNFalpha on host cell surface and recombinant fibroblast cell surface, leading to inhibition of biological functions of TNFalpha, overview
-
-
?
transferrin + H2O

hemin + ?
-
slight truncation of the polypeptide chain in serum
-
?
transferrin + H2O
hemin + ?
-
slight truncation of the polypeptide chain in serum
-
?
additional information

?
-
-
the enzyme makes a significant contribution to the virulence of Porphyromonas gingivalis
-
-
?
additional information
?
-
-
enzyme disrupts interaction between fibronectin and integrin in human fibroblasts, leading to cell death of detached fibroblasts, which contributes to the tissue damage in periodontal disease caused by Porphyromonas gingivalis
-
?
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
?
-
-
gingipains are essential for bacterial virulence and survival
-
-
?
additional information
?
-
-
gingipains cleave a broad range of in-host proteins and are key virulence factors in the onset and development of human adult periodontitis, the enzyme stimulates production of hepatocyte growth factor, i.e. scatter factor, through protease-activated receptors in human gingival fibroblasts in culture, overview
-
-
?
additional information
?
-
-
gingipains R are potent permeability enhancement factors by prekallikrein activation and bradykinin induction, the enzyme degrades proteins of connective tissue, cell surface proteins and receptors, cytokines and plasma proteins, including components of the coagulation and complement cascades, heme- and iron-binding proteins, immunoglobulins and proteinase inhibitors
-
-
?
additional information
?
-
-
gingipains R mediate coaggregation of Porphyromonas gingivalis with other bacteria, overview
-
-
?
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
-
-
?
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
?
-
-
implicated in a wide range of both pathological and physiological processes of Porphyromonas gingivalis, including destruction of periodontal tissue, disruption of host defense mechanisms, processing of bacterial cell surface and secretory proteins, and acquisition of heme and amino acids, involved in atherosclerotic processes
-
-
?
additional information
?
-
-
important for the provision of nutrients for the bacterium in the host organism, destruction of host tissue, modulation of host immune response
-
-
?
additional information
?
-
-
important virulence factors in periodontitis
-
-
?
additional information
?
-
-
important virulence factors in periodontitis
-
-
?
additional information
?
-
-
important virulence factors in periodontitis
-
-
?
additional information
?
-
-
important virulence factors in periodontitis
-
-
?
additional information
?
-
-
important virulence factors in periodontitis
-
-
?
additional information
?
-
-
important virulence factors in periodontitis, activation of the C1 complex in serum, degradation of multiple complement components, important factor for the resistance to the bacteriolytic activity of serum
-
-
?
additional information
?
-
-
important virulence factors in periodontitis, involved in the perturbation of host defense and the destruction and invasion of host tissues, degradation of hostâs proteins such as ICAM-1m VCAM-1, catenins, and cadherins, involved in the shedding of syndecan-1
-
-
?
additional information
?
-
-
important virulence factors in periodontitis, probably involved in the reduction of T-cell function at periodontal lesion sites, induction of PAR-1 and PAR-2 receptor expression, up-regulation of PAR-4 expression, little effect on PAR-3 expression, increases expression of CD69 and CD25 on T-cells
-
-
?
additional information
?
-
-
involved in the deregulation of the hostâs inflammatory response
-
-
?
additional information
?
-
-
involved in the induction of apoptosis in caspase dependent and caspase independent pathway
-
-
?
additional information
?
-
-
involved in the regulation of mRNA expression for the receptor activator of NF-kappaB ligand (RANKL) protein
-
-
?
additional information
?
-
-
no degradation of ICAM-3
-
-
?
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 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, overview
-
-
?
additional information
?
-
-
gingipains are involved in bacterial adherence to host cells, RgpA binds to adhesin via its adhesin binding domain. Peptide A44 derived from the adhesin domain of RgpA plays a role in binding of Porphyromonas gingivalis to HEP-2 epithelial cells via cell surface receptors, e.g. clathrin, nocodazole and paclitaxel, which disrupt microtubule formation, block the interaction, while genistein does not
-
-
?
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
?
-
-
HRgpA-mediated downregulation and RgpB-mediated upregulation of production of interleukin-8, occurs through protease-activated receptors, PAR-1 and PAR-2, signalling, RgpB-mediated upregulation of IL-8 production occurs through nuclear factor-kappa B, which does not affect HRgpA-mediated downregulation, overview. Gingipains preferentially suppress IL-8, resulting in attenuation of the cellular recognition of bacteria, and as a consequence, sustain chronic inflammation
-
-
?
additional information
?
-
-
enzyme disrupts interaction between fibronectin and integrin in human fibroblasts, leading to cell death of detached fibroblasts, which contributes to the tissue damage in periodontal disease caused by Porphyromonas gingivalis
-
?
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
?
-
-
gingipains cleave a broad range of in-host proteins and are key virulence factors in the onset and development of human adult periodontitis, the enzyme stimulates production of hepatocyte growth factor, i.e. scatter factor, through protease-activated receptors in human gingival fibroblasts in culture, overview
-
-
?
additional information
?
-
-
gingipains are essential for bacterial virulence and survival
-
-
?
additional information
?
-
-
HRgpA-mediated downregulation and RgpB-mediated upregulation of production of interleukin-8, occurs through protease-activated receptors, PAR-1 and PAR-2, signalling, RgpB-mediated upregulation of IL-8 production occurs through nuclear factor-kappa B, which does not affect HRgpA-mediated downregulation, overview. Gingipains preferentially suppress IL-8, resulting in attenuation of the cellular recognition of bacteria, and as a consequence, sustain chronic inflammation
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2,6-bis-(4-amidinobenzyl)-cyclohexanone
-
alpha2-Macroglobulin
-
-
-
benzamidine derivatives
-
overview, derivatives with an urea moiety linking the 2 aromatic rings, and derivatives with a less polar ether linker, the latter being less efficient inhibitors
bis-benzamidine with urea linker
-
best inhibitor
bovine pancreatic secretory trypsin inhibitor
-
i.e. PSTI bovine, about 33% inhibition at 0.0005 mM, 66% at 0.001 mM, and 87% at 0.0025 mM, a Kazal-type serine proteinase inhibitor purified from pancreas, bovine pancreatic secretory trypsin inhibitor having an essential Arg 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 Arg-specific gingipain R, whereas porcine inhibitor, possessing a Lys residue at the P1 position, exhibits activity only against the Lys-specific cysteine proteinase gingipain K, EC 3.4.22.47. The inhibitory effect is eliminated by Arg residue modification in 0.2 M borate buffer, pH 9.0, and 50 mM excess of cyclohexanedione in a 1 : 30 molar ratio at 37°C. The association equilibrium constant is 0.0016 mM
-
carbobenzoxy-Glu(NHN(CH3)Ph)-Lys-CO-NHCH2Ph
-
-
carbobenzoxy-Lys-Arg-CO-Lys-N(CH3)2
-
i.e. KYT-1, specific inhibition of Rgp, inhibits coaggregation of Porphyromonas gingivalis with other bacteria in vivo
carbobenzoxy-Lys-Arg-CO-Lys-N-(CH3)2
-
-
chicken ovoinhibitor
-
III and IV domains having Leu and Ser or Leu and Leu, respectively, at the P2' and P3' sites
-
Chloromethyl ketones
-
development of several inhibitor derivatives: structure-based design, chemistry, and activity, specificity for the Sn binding pocket of the enzyme, overview
Collagen type I
-
fibronectin and type I collagen addition inhibited the disruptive activity of the enzyme in human fibroblasts
-
D-arginine
-
complete inhibition of coaggregation of Porphyromonas gingivalis with other oral bacteria by L- and D-arginine
D-Phe-Phe-Arg-chloromethane
-
irreversible, strong inhibition
D-Phe-Phe-Arg-chloromethylketone
-
fast acting, irreversible alkylating inhibitor
D-Phe-Pro-Arg-chloromethane
-
irreversible, strong inhibition
D-Phe-Pro-Arg-chloromethyl ketone
-
Porphyromonas gingivalis treated with gingipain inhibitor do not induce buccal edema and gingivitis in BALB/c or C57BL/6 mice
doxycyclin
-
uncompetitive
doxycycline
-
strong inhibition
E-64
-
reversible inhibitor
E64
-
reversible, competitive inhibition
EGTA
-
completely reversed by addition of excess Ca2+
FA-70C1
-
potent inhibitor
fibronectin
-
fibronectin and type I collagen addition inhibited the disruptive activity of the enzyme in human fibroblasts
-
hemoglobin
-
prevents haptoglobin alpha-chain degradation in serum
-
Indocyanine green
Arg-gingipain is one of the important targets of indocyanine green as a photosensitizer
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
-
Kappaphycus alvarezii bromophenol
-
potent natural metabolite to control Porphyromas gingivalis induced infection
-
Kappaphycus alvarezii extract
-
potent natural metabolite to control Porphyromas gingivalis induced infection
-
L-arginine
-
complete inhibition of coaggregation of Porphyromonas gingivalis with other oral bacteria by L- and D-arginine
L-trans-epoxy-succinylleucylamido-(4-guanidino)butane
-
both enzyme forms
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; lactoferrin is incubated with purified RgpB which lacks the adhesin domains of RgA and Kgp. Lactoferrin inhibits RgpB activity by 77% at a concentration of 1.0 mg/ml and by 95% at 10 mg/ml confirming the inhibition is independent of adhesins
-
N-alpha-tosyl-L-lysyl chloromethyl ketone
Nalpha-p-tosyl-L-lysine chloromethyl ketone
-
TLCK
p-hydroxymercuribenzoate
-
complete inhibition at 0.2 mM, both enzyme forms
Phe-Arg-fluoromethylketone
-
-
Phe-Pro-Arg-chloroethyl ketone
-
FPR-cmk, inhibits Rgps
Phe-Pro-Arg-chloromethyl ketone
-
i.e. FPR-cmk, a specific inhibitor of Rgps, the inhibitor almost completely negates the RgpB-induced upregulation and HRgpA-induced downregulation
Phe-Pro-Arg-chloromethylketone
-
-
Pro-Phe-Arg-chloromethylketone
-
-
prodomain of arginine-specific gingipain A
-
-
-
prodomain of arginine-specific gingipain B
-
-
-
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
-
RLMAAKAESRK
competitive inhibitor
RRLMAAKAES
mixed-type inhibitor
RRLMAAKAESR
mixed-type inhibitor
RRLMAAKAESRK
mixed-type inhibitor, the arginine residue at position 15 of the docapeptide substantially contributes to the enzyme-inhibitory activity and the arginine residue at position 14 plays important roles in exerting enzyme-inhibitory activity
tetracyclin
-
uncompetitive
tosyl-L-Lys chloromethyl ketone
-
i.e. TLCK
tosyl-L-lysine chloromethyl ketone
-
i.e. TLCK, both enzyme forms
tosyl-L-lysyl-chloromethylketone
-
-
tosyl-L-Phe chloromethyl ketone
-
i.e. TPCK
YPR-chloromethylketone
-
-
Z-FFR-chloromethylketone
-
-
antipain

-
both enzyme forms
benzamidine

-
-
Chlorhexidine

-
strong inhibition
Chlorhexidine
-
synergistic effect of Zn2+ in a 1:1 ratio of chlorhexidine and Zn2+
EDTA

-
-
EDTA
-
completely reversed by addition of excess Ca2+
iodoacetamide

-
-
iodoacetamide
-
irreversible inhibition
iodoacetic acid

-
-
iodoacetic acid
-
irreversible inhibition
KYT-1

-
specific Rgp inhibitor
KYT-1
-
specific inhibitor
KYT-1
-
i.e. Cbz-Lys-Arg-CO-Lys-N(NH3)2
KYT-1
-
specific inhibitor, complete inhibition at 0.01 mM
leupeptin

-
both enzyme forms
leupeptin
-
strong inhibition
leupeptin
-
inhibits Arg-specific Rgp, but not Lys-specific Kgp
leupeptin
-
a specific arginine-gingipain inhibitor
leupeptin
-
human gingvial epithelial cells treated with Rgp-specific inhibitor leupeptin and challenged with Porphyromonas gingivalis cells do not undergo apoptosis
N-alpha-tosyl-L-lysyl chloromethyl ketone

-
TLCK
N-alpha-tosyl-L-lysyl chloromethyl ketone
-
-
N-ethylmaleimide

-
both enzyme forms
N-ethylmaleimide
-
irreversible inhibition
Zn2+

-
complete inhibition of both enzyme forms at 6.7 mM, increases inhibitory effect of benzamidine derivatives 2-3fold, lowers Ki-values, binding mechanism
additional information

-
resistant to inhibition by proteinase inhibitors in human plasma
-
additional information
-
no inhibition by aprotinin, epsilon-aminocaproic acid and diisopropylfluorophosphate
-
additional information
-
enzyme activity and cleavage pattern are not affected by 0.1% SDS, 1% Triton X-100, 1% octyl- and decylpyranoside
-
additional information
-
no or nearly no inhibition by cathepsin B inhibior II, metronidazole, peicillin G, and erythromycin
-
additional information
-
RgpB is stable to denaturing agents, e.g. urea, SDS, Triton X-100, and 1% octyl or decylpyranoside
-
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
-
the prodomain of lysine-specific gingipain shows no inhibitory activity
-
additional information
-
protein extracts from polished rice inhibit the proteolytic activity of the enzyme
-
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malfunction

-
human keratinocyte Rgp-deficient and Kgp-deficient double mutant cells do not cleave protease-activated recptor-1 and -2. The single Rgp-negative mutant cleaves protease-activated recptor-2
malfunction
-
Porphyromonas gingivalis double mutant RgpA/RgpB cells do not induce apoptosis in human gingvial epithelial cells
malfunction
-
Porphyromonas gingivalis RgpA/B double mutant do not induce buccal edema and gingivitis in BALB/c or C57BL/6 mice
malfunction
-
Porphyromonas gingivalis secretes outer membrane vesicles that contain major virulence factors, including Arg-gingipain and Lys-gingipain. Proteolytic activity of Rgp is required for membrane vesicles entry. Only few Rgp-null membrane vesicles enter the cells, and these negligibly degrade transferrin receptor, whereas paxillin and focal adhesion kinase degradation is significant
malfunction
-
the roles of several virulence factors in homotypic biofilm development by Porphyromonas gingivalis. A RgpA/B double mutant develops channel-like biofilms with fibrillar and tall microcolonies in PBS. When this mutant is studied in diluted trypticase soy broth, there is an increase in the number of peaks and the morphology changed to taller and loosely packed biofilms. Results suggests that Rgp controlls microcolony morphology and biovolume 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
metabolism

-
methaemoglobin formation by R-gingipain facilitates extraction of haem from haemoglobin by HmuY (haem-binding protein)
metabolism
-
the presence of Rgps promotes caspase-1 activation. The caspase-1-dependent interleukin-1beta response is cooperatively diminished by isoforms RgpA and RgpB
metabolism
-
the presence of Rgps promotes caspase-1 activation. The caspase-1-dependent interleukin-1beta response is cooperatively diminished by isoforms RgpA and RgpB
-
physiological function

-
cysteine-activated arginine gingipain RgpB sensitizes erythrocytes to the haemolytic effect of the K2 domain of Kgp (Lys-gingipain). RgpB degrades glycophorin A thereby potentially exposing the closely associated band 3 protein on the erythrocyte surface
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) but not low molecular weight gingipain (RgpB) mediate strong upregulation of the expression of pro-inflammatory cytokines (interleukin-1beta and colony stimulatory factor) in macrophages
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
-
Porphyromonas gingivalis W83 (wild type), but not gingipain-deficient mutant or wild-type bacteria pretreated with gingipain inhibitors, elicit buccal edema and gingivitis in BALB/c or C57BL/6 mice. Studies in Toll-like receptors 2-/-, bradykinin B2 receptor -/-, and neutrophil-depleted C57BL/6 mice reveal that Porphyromonas gingivalis induce edema through the sequential activation of Toll-like receptors 2/neutrophils, with the initial plasma leakage being amplified by gingipain-dependent release of vasoactive kinins from plasma-borne kininogens
physiological function
-
Rgp-cleavage of protease-activated receptor-1 up-regulates expression of cytokines
physiological function
-
results suggest that gingipains may have a role in the resistance of Porphyromonas gingivalis ATCC 49417 to human beta-defensin 3
physiological function
-
Arg-gingipain promotes the aggregation of Treponema denticola in multi-species biofilms
physiological function
isoform RgbB is an odontopathogenic virulence factor
physiological function
-
the activity of the gingipains on the inflammatory and immune response of human gingival fibroblasts are crucial in periodontitis
physiological function
-
the enzyme plays a significant role in induction and regulation of CXCL8 in THP-1 cells
physiological function
-
the isoforms RgpA and RgbB play a critical role in Akt dephosphorylation and inhibit the PI3K/Akt signaling pathway
physiological function
-
major virulence factors in Porphyromas gingivalis
physiological function
-
Arg-gingipain promotes the aggregation of Treponema denticola in multi-species biofilms
-
physiological function
-
isoform RgbB is an odontopathogenic virulence factor
-
physiological function
-
the enzyme plays a significant role in induction and regulation of CXCL8 in THP-1 cells
-
physiological function
-
the activity of the gingipains on the inflammatory and immune response of human gingival fibroblasts are crucial in periodontitis
-
additional information

-
the maturation pathways for RgpA and RgpB are different, the late onset gingipains activity in the vimA-defective mutant is due to activation/maturation of RgpB. The activation of RgpB can involve autolytic processing
additional information
the maturation pathways for RgpA and RgpB are different, the late onset gingipains activity in the vimA-defective mutant is due to activation/maturation of RgpB. The activation of RgpB can involve autolytic processing
additional information
-
the maturation pathways for RgpA and RgpB are different. RgpA activity can be activated in the absence of RgpB. RgpA is VimA-dependent
additional information
the maturation pathways for RgpA and RgpB are different. RgpA activity can be activated in the absence of RgpB. RgpA is VimA-dependent
additional information
-
the maturation pathways for RgpA and RgpB are different. RgpA activity can be activated in the absence of RgpB. RgpA is VimA-dependent
-
additional information
-
the maturation pathways for RgpA and RgpB are different, the late onset gingipains activity in the vimA-defective mutant is due to activation/maturation of RgpB. The activation of RgpB can involve autolytic processing
-
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?

-
x * 43000, both enzyme forms, SDS-PAGE
?
-
native and C244A mutant enzyme expressed with numerous bands, 80000-9000 Da, SDS-PAGE
?
-
truncated enzyme expressed as 71000 Da and 48000 Da isoforms, SDS-PAGE
?
-
x * 56000, RgpB, calculated from the deduced amino acid sequence
?
x * 45000, isoform RgpB, SDS-PAGE
?
-
x * 48000, low molecular weight gingipain B, SDS-PAGE
?
-
x * 48200, MALDI TOF mass spectrometry
?
-
x * 95000, high molecular weight gingipain A, SDS-PAGE
?
x * 98000, isoform HRgpA, SDS-PAGE
?
-
x * 45000, isoform RgpB, SDS-PAGE
-
?
-
x * 98000, isoform HRgpA, SDS-PAGE
-
?
-
x * 48000, low molecular weight gingipain B, SDS-PAGE
-
?
-
x * 95000, high molecular weight gingipain A, SDS-PAGE
-
?
-
x * 48200, MALDI TOF mass spectrometry
-
?
-
x * 45000, isoform RgpB, SDS-PAGE
-
dimer

-
heterodimer, HRgpA
dimer
-
heterodimeric RgpA fused to adhesin, i.e. HRgpA
dimer
-
heterodimer, HRgpA
-
monomer

-
1 * 50000, Porphyromonas gingivalis, SDS-PAGE
monomer
1 * 48019-48369, gingipain R2 isozymes I-IV and laser mass spectroscopy
monomer
1 * 48019-48369, gingipain R2 isozymes I-IV, laser mass spectroscopy
monomer
-
1 * 48000, RgpB, SDS-PAGE
monomer
-
1 * 48000, RgpB, SDS-PAGE
-
monomer
-
1 * 48019-48369, gingipain R2 isozymes I-IV and laser mass spectroscopy
-
monomer
-
1 * 48019-48369, gingipain R2 isozymes I-IV, laser mass spectroscopy
-
additional information

-
crystal structure analysis
additional information
-
molecular modeling of the catalytic domain structure of HRgpA based on the RgpB structure, isoforms HRgpA and RgpB, the first containing 4 amino acid changes compared to the latter, which are D281N, Y283S, P286S, and N331K that all map to the region surrounding the active site
additional information
-
the enzyme complex consists of 4 major polypeptides of 49.5 kDa for the catalytic domain, 43 kDa, 23.3 kDa, and 15.9 kDa
additional information
the enzyme complex consists of 4 major polypeptides of 49.5 kDa for the catalytic domain, 43 kDa, 23.3 kDa, and 15.9 kDa
additional information
the enzyme complex consists of 4 major polypeptides of 49.5 kDa for the catalytic domain, 43 kDa, 23.3 kDa, and 15.9 kDa
additional information
-
Rgp possesses C-terminal a hemagglutinin domain containing the proteins responsible for coaggregation activity of Porphyromonas gingivalis, overview
additional information
-
RgpA and Kgp proteinase polyprotein domain structure, peptide mass fingerprinting and mass spectrometry, overview
additional information
-
RgpA can occur as monomer or as heterodimer fused to adhesins and a hemagglutinin domain, while RgpB possesses only a small hemagglutinin domain, domain structure, overview
additional information
-
structure analysis, gingipain R occurs in different forms of 50-110 kDa, tertiary structure, the C-terminus shows an IgSF-like fold, overview
additional information
-
RgpA possesses an adhesin domain
additional information
-
x * 95000, HRgpA, SDS-PAGE, 50000, RgpB, SDS-PAGE
additional information
-
crystal structure analysis
-
additional information
-
the enzyme complex consists of 4 major polypeptides of 49.5 kDa for the catalytic domain, 43 kDa, 23.3 kDa, and 15.9 kDa
-
additional information
-
x * 95000, HRgpA, SDS-PAGE, 50000, RgpB, SDS-PAGE
-
additional information
-
RgpA and Kgp proteinase polyprotein domain structure, peptide mass fingerprinting and mass spectrometry, overview
-
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