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Enzyme Nomenclature
Information on EC 3.4.22.37 - gingipain R
Word Map on EC 3.4.22.37
- 3.4.22.37
- gingivalis
- porphyromonas
- periodontal
-
proteinases
-
adhesins
-
lysine-specific
-
hemagglutinins
-
protease-activated
-
periodontopathogenic
-
hemagglutination
-
black-pigmented
-
fimbriae
-
crevicular
- pharmacology
-
gliding
- medicine
- molecular biology
- drug development
-
gingivalis-induced
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autoaggregation
- biotechnology
-
coaggregation
-
bacteroidetes
- diagnostics
- johnsoniae
-
lys-specific
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The expected taxonomic range for this enzyme is: Porphyromonas gingivalis
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EC NUMBER 
COMMENTARY 
3.4.22.37
-
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RECOMMENDED NAME
GeneOntology No.
gingipain R
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrolysis of proteins and small molecule substrates, with a preference for Arg in P1
-
-
-
-
hydrolysis of proteins and small molecule substrates, with a preference for Arg in P1
Cys244-His211 catalytic diad and a nearby Glu arranged around the S1 specificity pocket, which carries an Asp residue to enforce preference for Arg-P1 residues, mechanism and binding mode at the active site
-
hydrolysis of proteins and small molecule substrates, with a preference for Arg in P1
proteolysis of selected proteins
hydrolysis of proteins and small molecule substrates, with a preference for Arg in P1
active site structure
-
hydrolysis of proteins and small molecule substrates, with a preference for Arg in P1
active site structure, role of the Sn binding pocket, molecular basis for substrate specificity
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hydrolysis of proteins and small molecule substrates, with a preference for Arg in P1
proteolysis of selected proteins
-
-
hydrolysis of proteins and small molecule substrates, with a preference for Arg in P1
active site structure, role of the Sn binding pocket, molecular basis for substrate specificity; Cys244-His211 catalytic diad and a nearby Glu arranged around the S1 specificity pocket, which carries an Asp residue to enforce preference for Arg-P1 residues, mechanism and binding mode at the active site
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
-
-
-
-
hydrolysis of peptide bond
-
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CAS REGISTRY NUMBER
COMMENTARY
159745-71-8
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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30348, 30349, 30350, 30352, 653818, 670453, 686175, 697195, 697200, 699738, 705382, 707889, 707890, 708520, 708710, 708711, 709355, 709393, 709671, 709842, 710002, 717084, 717097, 717099, 718188, 718267, 731334, 731337, 731408, 731503, 731555, 731556, 731625, 731779, 731810, 732100, 732183, 732537, 732539
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genes rgpA and rgpB, wild-type strain W50, RgpA-deficient isogenic strain W501, and RgpB-deficient isogenic strain D7
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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
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strain ATCC 33277, 2 arginine-specific gingipains RGP-A and RGP-B
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strain ATCC33277, gene rgpB gene, enzyme gingipain R2, 4 isoforms I-IV that are indistinguishable with regard to stability, pH-optima, kinetic characteristics and proteolytic activity
UniProt
strain ATCC33277, wild-type and 4 enzyme-deficient mutants, isozymes gingipains A and B, encoded by the genes rgpA and rgpB
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strain HG66, gene rgpB/rgp-2 gene, enzyme gingipain R2, 4 isoforms I-IV that are indistinguishable with regard to stability, pH-optima, kinetic characteristics and proteolytic activity
SwissProt
strains ATCC 33277 (wild type), the Rgp/Kgp-null (rgpA rgpB kgpdeficient) triple-mutant KDP136, the Kgp-null (kgp) mutant (KDP129),and an Rgp-null (rgpA rgpBdeficient) double-mutant (KDP133)
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strains ATCC33277, a gingipain null mutant (KDP136), and a fimbria-null mutant (KDP150)
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strains W83 and FLL203 which is a periplasemic heat-shock serine protease, both strains grow at similar rate at 37°C but at 42°C the FLL203 strains grows more slowly and not over an OD600 of 0.9, heat treatment of bacteria at 55°C results in an upregulation of the enzyme activity in W83 and a decrease in activity in FLL203
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strains W83, 83K3 which is deficient in the sov gene that seems be required for the export of RgpB through the outer membrane
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wild-type strain W50, and enzyme-deficient strains D7, W501, and E8, genes rgpA and rgpB
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strain ATCC33277, gene rgpB gene, enzyme gingipain R2, 4 isoforms I-IV that are indistinguishable with regard to stability, pH-optima, kinetic characteristics and proteolytic activity
UniProt
strain ATCC33277, wild-type and 4 enzyme-deficient mutants, isozymes gingipains A and B, encoded by the genes rgpA and rgpB
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strain HG66, gene rgpB/rgp-2 gene, enzyme gingipain R2, 4 isoforms I-IV that are indistinguishable with regard to stability, pH-optima, kinetic characteristics and proteolytic activity
SwissProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
Porphyromonas gingivalis double mutant RgpA/RgpB 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 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
malfunction
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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
-
Porphyromonas gingivalis RgpA/B double mutant do not induce buccal edema and gingivitis in BALB/c or C57BL/6 mice
malfunction
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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
metabolism
-
methaemoglobin formation by R-gingipain facilitates extraction of haem from haemoglobin by HmuY (haem-binding protein)
metabolism
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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
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physiological function
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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
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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
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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
-
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; 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
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gingipains induce the degradation and inactivation of endothelial thrombomodulin which may promote vascular coagulation and inflammation
physiological function
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Rgp-cleavage of protease-activated receptor-1 up-regulates expression of cytokines
physiological function
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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
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results suggest that gingipains may have a role in the resistance of Porphyromonas gingivalis ATCC 49417 to human beta-defensin 3
physiological function
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the enzyme plays a significant role in induction and regulation of CXCL8 in THP-1 cells
physiological function
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Arg-gingipain promotes the aggregation of Treponema denticola in multi-species biofilms
physiological function
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isoform RgbB is an odontopathogenic virulence factor
physiological function
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the isoforms RgpA and RgbB play a critical role in Akt dephosphorylation and inhibit the PI3K/Akt signaling pathway
physiological function
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the activity of the gingipains on the inflammatory and immune response of human gingival fibroblasts are crucial in periodontitis
physiological function
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the activity of the gingipains on the inflammatory and immune response of human gingival fibroblasts are crucial in periodontitis; the enzyme plays a significant role in induction and regulation of CXCL8 in THP-1 cells
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physiological function
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Arg-gingipain promotes the aggregation of Treponema denticola in multi-species biofilms
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physiological function
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isoform RgbB is an odontopathogenic virulence factor
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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
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
-
?
apoB-100 protein + H2O
?
-
apoB-100 degradation induces LDL-modification and contributes to the onset of atherosclerosis
-
-
?
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-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
-
-
-
?
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
?
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involved in the detachment of endothelial cells
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-
?
denatured alpha1-proteinase inhibitor + H2O
?
-
-
?
factor IX proenzyme + H2O
?
-
activation through limited proteolysis
-
-
?
factor X proenzyme + H2O
?
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activation through limited proteolysis
-
-
?
fibrinogen A alpha-chain + H2O
28 kDa fragment + ?
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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
?
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the enzyme isoforms HRgpA and RgpB effectively destroy the cell-binding domain of fibronectin
-
-
?
haemoglobin + H2O
?
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complete digestion, enzyme form RGP-B shows high activity, not RGP-A, human substrate
-
?
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
-
?
N-alpha-benzoyl-D,L-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + 4-nitroanilide
-
-
-
-
?
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
-
-
?
Nalpha-benzoyl-D,L-Arg-4-nitroanilide + H2O
Nalpha-benzoyl-D,L-Arg + 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
-
-
-
-
?
prefimbrillin + H2O
fimbrilline + ?
-
-
mature form of the protein
-
?
protease-activated receptor-1 + H2O
?
-
specific substrate for Arg-gingipain
-
-
?
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
-
-
?
ribonuclease A + H2O
?
-
absolutely specific cleavage of all Arg-Xaa peptides bonds
-
?
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
-
?
transferring receptor + H2O
?
-
Rgp is responsible for transferring receptor degradation
-
-
?
Z-Arg-Arg-4-nitroanilide + H2O
Z-Arg-Arg + 4-nitroaniline
synthetic fluorogenic substrate
-
?
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
?
synthetic chromogenic substrate
-
?
azocasein + H2O
?
synthetic chromogenic substrate
-
?
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
-
?
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 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
?
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
-
-
?
human protease-activated receptor PAR-2 + H2O
?
-
PAR-2 activation on epithelial cells
-
-
?
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
-
-
?
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
-
-
?
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 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 + ?
-
slight truncation of the polypeptide chain in serum
-
?
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 hosts 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 hosts 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
?
-
-
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.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
apoB-100 protein + H2O
?
-
apoB-100 degradation induces LDL-modification and contributes to the onset of atherosclerosis
-
-
?
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
-
-
?
human protease-activated receptor PAR-2 + H2O
?
-
PAR-2 activation on epithelial cells
-
-
?
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
-
-
?
prefimbrillin + H2O
fimbrilline + ?
-
-
mature form of the protein
-
?
protease-activated receptor-1 + H2O
?
-
specific substrate for Arg-gingipain
-
-
?
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
-
-
?
transferring receptor + H2O
?
-
Rgp is responsible for transferring receptor degradation
-
-
?
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
-
?
elafin + H2O
?
P28784, P95493
all three gingipains have the ability to degrade elafin (endogenous inhibitor secreted by epithelial cells)
-
-
?
elafin + H2O
?
P28784, P95493
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
?
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
-
-
?
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
-
-
?
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 hosts 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 hosts 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
?
-
-
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.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
additional information
-
enzyme forms are not affected by Mg2+ and Ca2+
Ca2+
-
activation of prothrombin cleavage in presence of phospholipids by HRgpA not RgpB
Ca2+
-
stabilizes all forms of gingipain R, not necessary for activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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-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
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-chloromethylketone
-
fast acting, irreversible alkylating inhibitor
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
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
-
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
-
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
-
p-hydroxymercuribenzoate
-
complete inhibition at 0.2 mM, both enzyme forms
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
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
-
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
-
Chlorhexidine
-
synergistic effect of Zn2+ in a 1:1 ratio of chlorhexidine and Zn2+
leupeptin
-
human gingvial epithelial cells treated with Rgp-specific inhibitor leupeptin and challenged with Porphyromonas gingivalis cells do not undergo apoptosis
leupeptin
-
-
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Phospholipids
-
activation of prothrombin cleavage in presence of Ca2+ by HRgpA not RgpB, 1.5fold at 0.04 mg/ml
Urea
-
3fold activation at 6 M, probably due to unfolding of the substrate azocasein, which enhances the enzymes sensitivity for proteolytic cleavage
2-mercaptoethanol
weak activation, a concentration above 100 mM is required
cysteine
10 mM, most effective reducing agent for activation of the enzyme, denaturation occurs at higher concentration above 5 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
dithiothreitol
weak activation, a concentration above 100 mM is required
glycyl-glycine
-
increases the substrate hydrolysis, increases Km and kcat value
glycyl-glycine
stimulates the amidolytic activity and limited proteolysis, but destabilizes the enzyme; stimulates the amidolytic activity and limited proteolysis, but destabilizes the isozymes
additional information
-
human serum minimal medium induces enzyme expression
-
additional information
-
enzyme activity and cleavage pattern are not affected by 0.1% SDS, 1% Triton X-100, or 1% octyl- and 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. Synergistic effects of gingipains and, synthetic TLR or NOD ligands on secretion of proinflammatory cytokines in cultured human peripheral blood mononuclear cellshuman peripheral blood mononuclear cells
-
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
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00026
prothrombin
-
HRgpA, pH 7.6, 37°C, in presence of Ca2+ and phospholipids
-
0.0066
prothrombin
-
RgpB, pH 7.6, 37°C, in presence of Ca2+ and phospholipids
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.076
prothrombin
-
RgpB, pH 7.6, 37°C, in presence of Ca2+ and phospholipids
-
0.32
prothrombin
-
HRgpA, pH 7.6, 37°C, in presence of Ca2+ and phospholipids
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0029
2,6-bis-(4-amidinobenzyl)-cyclohexanone
at pH 7.6 and 37°C; at pH 7.6 and 37°C
-
0.536
benzamidine
at pH 7.6 and 37°C; at pH 7.6 and 37°C
0.005
lactoferrin
-
pH 8.0, 37°C, a kinetic analysis of the inhibition of Arg-specific proteolytic activity of purified gingivalis RgpA/Kgp proteinase-adhesin complexes by lactoferrin demonstrates time-dependent inhibition with a first-order inactivation rate constant (kinact) of 0.023/min
-
0.107
Pentamidine
at pH 7.6 and 37°C; at pH 7.6 and 37°C
0.013
bis-benzamidine with urea linker
-
pH 7.6, RgpB, in presence of Zn2+
0.015
bis-benzamidine with urea linker
-
pH 7.6, HRgpA, in presence of Zn2+
0.03
bis-benzamidine with urea linker
-
pH 7.6, HRgpA and RgpB, in absence of Zn2+
0.00000085
prodomain of arginine-specific gingipain A
-
isoform HRgpA, in 200 mM Tris-HCl, 5 mM CaCl2, 150 mM NaCl, and 0.02% (w/v) NaN3, pH 7.6, supplemented with 10 mM L-cysteine, at 37°C
-
0.0000021
prodomain of arginine-specific gingipain A
-
isoform RgpB, in 200 mM Tris-HCl, 5 mM CaCl2, 150 mM NaCl, and 0.02% (w/v) NaN3, pH 7.6, supplemented with 10 mM L-cysteine, at 37°C
-
0.0000053
prodomain of arginine-specific gingipain B
-
isoform HRgpA, in 200 mM Tris-HCl, 5 mM CaCl2, 150 mM NaCl, and 0.02% (w/v) NaN3, pH 7.6, supplemented with 10 mM L-cysteine, at 37°C
-
0.0000062
prodomain of arginine-specific gingipain B
-
isoform RgpB, in 200 mM Tris-HCl, 5 mM CaCl2, 150 mM NaCl, and 0.02% (w/v) NaN3, pH 7.6, supplemented with 10 mM L-cysteine, at 37°C
-
additional information
additional information
-
Ki-values for benzamidine derivatives in presence or absence of Zn2+
-
additional information
additional information
-
inhibition kinetics, overview
-
additional information
additional information
-
inhibition kinetics
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000071
prodomain of arginine-specific gingipain B
Porphyromonas gingivalis
-
isoform RgpB, with azocoll as substrate, in 200 mM Tris-HCl, 5 mM CaCl2, 150 mM NaCl, and 0.02% (w/v) NaN3, pH 7.6, supplemented with 10 mM L-cysteine, at 37°C
-
0.0000072
prodomain of arginine-specific gingipain B
Porphyromonas gingivalis
-
isoform RgpB, with H-Arg-7-amido-4-methylcoumarin as substrate, in 200 mM Tris-HCl, 5 mM CaCl2, 150 mM NaCl, and 0.02% (w/v) NaN3, pH 7.6, supplemented with 10 mM L-cysteine, at 37°C
-
0.0000237
prodomain of arginine-specific gingipain B
Porphyromonas gingivalis
-
isoform RgpB, with Nalpha-benzoyl-L-arginine 4-nitroanilide as substrate, in 200 mM Tris-HCl, 5 mM CaCl2, 150 mM NaCl, and 0.02% (w/v) NaN3, pH 7.6, supplemented with 10 mM L-cysteine, at 37°C
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
quantification of hepatocyte growth factor induction by RgpB and HRgpA
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
9.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9.5
5 - 9.5
50% activity at pH 5.0, maximal activity at pH 9.5
5 - 9.5
-
isoform RgpB has a broad pH optimum in the range of pH 9.5 (100% activity) down to pH 5.0 (50%)
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 37
-
with denatured substrate collagen type I, native collagen type I is only degraded at 37°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.1
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
outer membrane protein Sov participates in the secretion of Arg-gingipain. Secretion is Rgp inhibited by anti-Sov antiserum raised against the C-terminal region of Soc
-
Porphyromonas gingivalis secretes outer membrane vesicles that contain major virulence factors, including Arg-gingipain and Lys-gingipain
additional information
-
in extracellular vesicles and soluble in the culture supernatant
-
additional information
-
localization pattern in strain FLL203 is affected upon cell growth at 42°C
-
additional information
-
gingipain adhesin domains are involved in targeting their associated proteolytic activities to cell surface receptors, colocalization of the arg-gingipain, RgpA, adhesin domain with fibronectin and the alpha5beta1 integrin receptor for fibronectin
-
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45000
48000
48120 - 48150
mature, C-terminally truncated isozymes, amino acid sequence calculation and mass spectroscopy; mature, C-terminally truncated isozymes, amino acid sequence calculation, gel filtration and mass spectroscopy
50000
56000
-
x * 56000, RgpB, calculated from the deduced amino acid sequence
95000
additional information
-
the enzyme exists as multiple MW species. The major forms are: 110000 MW, 95000 MW, 70000-90000 MW, and 50000 MW. The first two being a complex of the 50000 MW catalytic subunit with hemagglutinins, with or without an added membrane anchorage peptide. The other forms are single-chain enzymes. The 95000 MW and the 50000 MW form are found predominantly in culture medium, the 110000 and 70000-90000 MW foms are associated with membranous fractions of the bacteria
45000
x * 45000, isoform RgpB, SDS-PAGE; x * 45000, isoform RgpB, SDS-PAGE
95000
a complex of catalytic and hemagglutinin/adhesin domains, gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
additional information
?
-
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 * 48000, low molecular weight gingipain B, SDS-PAGE; x * 95000, high molecular weight gingipain A, SDS-PAGE
?
x * 45000, isoform RgpB, SDS-PAGE; x * 45000, isoform RgpB, 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 * 48200, MALDI TOF mass spectrometry; x * 95000, high molecular weight gingipain A, SDS-PAGE
-
monomer
1 * 48019-48369, gingipain R2 isozymes I-IV and laser mass spectroscopy; 1 * 48019-48369, gingipain R2 isozymes I-IV, laser mass spectroscopy
monomer
-
1 * 48000, RgpB, SDS-PAGE; 1 * 48019-48369, gingipain R2 isozymes I-IV and laser mass spectroscopy; 1 * 48019-48369, gingipain R2 isozymes I-IV, laser mass spectroscopy
-
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
-
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 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
-
x * 95000, HRgpA, SDS-PAGE, 50000, RgpB, SDS-PAGE
additional information
-
crystal structure analysis; 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; 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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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
glycoprotein
-
monosaccharide composition of RgpA, expression of RgpB is required for correct glycosylation and stability of monomeric RgpA from strain W50
proteolytic modification
the mature enzyme is C-terminally truncated to 433 amino acid residues
proteolytic modification
-
gingipain R performs autoprocessing and activation to mature enzyme, overview
proteolytic modification
-
RgpA and Kgp proteinases are synthesized as a polyprotein and proteolytically processed to individual proteinases and adhesins, C-terminal processing by carboxypeptidase CPG70
proteolytic modification
-
the mature enzyme is C-terminally truncated to 433 amino acid residues
-
proteolytic modification
-
RgpA and Kgp proteinases are synthesized as a polyprotein and proteolytically processed to individual proteinases and adhesins, C-terminal processing by carboxypeptidase CPG70
-
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified enzyme gingipain R2 in complex with fast acting, irreversible inhibitor H-D-Phe-Phe-Arg-chloromethylketone, activated by incubation for 30 min in 0.1 M HEPES, pH 8.0, 10 mM L-cysteine, 2.5 mM CaCl2, at 37°C, alkylation of the active site cysteine by addition of inhibitor, crystallization by sitting-drop vapour diffusion method at 20°C, different protein-inhibitor complex solution systems using PEG 8000 as precipitant for 10 mg/ml protein, X-ray diffraction structure determination at 2.9 A resolution and analysis
-
purified RgpB free or in complex with fast acting, irreversible inhibitor D-Phe-Phe-Arg-chloromethylketone, activated by incubation for 30 min in 0.1 M HEPES, pH 8.0, 10 mM L-cysteine, 2.5 mM CaCl2, at 37°C, alkylation of the active site cysteine by addition of inhibitor, crystallization of dialysed sample by vapour diffusion method, 8 mg/ml protein in 3 mM MOPS, pH 7.2 0.02% NaN3, plus equal volume of reservoir solution: 3.4 M 1,6-hexandiol, 0.2 M MgCl2, 0.1 M Tris-HCl, pH 8.5, at 21°C, several weeks, X-ray diffraction structure determination at 1.5-2.16 A resolution and analysis, structure modeling
-
sitting drop vapor diffusion method, using 14% (w/v) polyethylene glycol 6000, 0.1 M sodium acetate, pH 5.0, 0.2 M calcium chloride as reservoir solution
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.8 - 8.3
-
stability of RgpA catalytic domain of wild-type and D7 mutant strain at 30°C in absence or presence of 2-mercaptoethanol or Ca2+, overview
668922
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
-
50 mM Tris,-HCl, pH 7.8, 10 min, remaining activity for RGP-A is 82% and for RGP-B 52% of maximal activity, after 30 min remaining activity for RGP-A is 58% and for RGP-B 26% of maximal activity
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Ca2+ stabilizes the enzyme, while glycyl-glycine destabilizes the enzyme
Ca2+ stabilizes the isozymes, while glycyl-glycine destabilizes the isozymes
expression of RgpB is required for correct glycosylation and stability of monomeric RgpA from strain W50
-
RgpB is stable and active in buffers containing 6 M urea, 0.1% SDS, 1% Triton X-100, and 1% octyl or decylpyranoside
-
RgpB is stable to denaturing agents, e.g. urea, SDS, Triton X-100, and 1% octyl or decylpyranoside
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, buffer with neutral pH, 1-5 mM CaCl2, indefinitely stable
0°C, on ice, buffer with neutral pH, 1-5 mM CaCl2, stable for months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetone sulfate precipitation, arginine-Sepharose column chromatography, and Sephadex G-150 gel filtration
-
arginine-Sepharose column chromatography, Mono Q column chromatography, and gel filtration
-
benzamidine-Sepharose column chromatography and Sephadex G-25 gel filtration; benzamidine-Sepharose column chromatography and Sephadex G-25 gel filtration
enzyme form Arg-gingivain-75, Arg-gingivain-70 and Arg-gingivain-55
-
from cell culture medium; isozymes I-IV from cell culture medium, 4.5-5fold
glutathione-Sepharose column chromatography and Superdex 75 gel filtration
-
native enzyme from envelope and/or outer membranes by ammonium sulfate or acetone precipitation, ion exchange chromatography, gel filtration, isoelectric or chromatofocusing, and affinity chromatography
-
native enzymes by ammonium sulfate fractionation, ion exchange and affinity chromatography, RgpA and RgpB by different methods, overview
-
RGP-A and RGP-B, from envelope material, solubilization by detergent 3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate, i.e. CHAPS
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
different enzyme fragments expressed as His-tag fusion proteins in Escherichia coli BL21(DE3)
-
expression of wild-type and mutant enzymes in murine ST2 osteoblastic/stromal cells
-
RgpB as a full-length zymogen, with a catalytic Cys244Ala mutation, or with the C-terminal 72 amino acids deleted in an Arg-gingipain Porphyromonas gingivalis mutant (YH522AB) and an Arg- and Lys-gingipain mutant (YH522KAB)
-
RgpB with the C-terminal His-tag is produced by the Porphyromonas gingivalis W83 strain bearing the modified rgpB gene
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DELTA435-507
-
largely inactive, incorrect localization in culture supernatant and periplasm
additional information
additional information
-
4 naturally occuring enzyme deficient mutants: rgpA-deficient mutant shows 77% activity compared to the wild-type activity with type I collagen, while a rgpB-deficent mutant shows 82% activity, and a double-deficient mutant strain shows only 6% activity, another mutant lacking the to arginine-specific isozyme and the lysine-specific gingipain KGP shows 5% remaining activity
additional information
-
strain W501 is deficient for RgpA, strain E8 for Rgp, and strain D7 for RgpB
additional information
-
mutant RgpA-deficient isogenic strain W501 and RgpB-deficient isogenic strain D7 show 50% of wild-type strain W50 enzyme activity
additional information
-
Rgp null mutant strain KDP133 shows platelet aggregation similar to the wild-type strain ATCC 33277, while neither the Rgp/Kgp null mutant strain, nor the adhesin null mutant strain show platelet 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 KDP137 phenotypes, overview
additional information
-
construction of enzyme-deficient mutants KDP136 with DELTArgpADELTArgpBDELTAkgp, and KDP133 with DELTAkgp. 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
-
4 naturally occuring enzyme deficient mutants: rgpA-deficient mutant shows 77% activity compared to the wild-type activity with type I collagen, while a rgpB-deficent mutant shows 82% activity, and a double-deficient mutant strain shows only 6% activity, another mutant lacking the to arginine-specific isozyme and the lysine-specific gingipain KGP shows 5% remaining activity; construction of enzyme-deficient mutants KDP136 with DELTArgpADELTArgpBDELTAkgp, and KDP133 with DELTAkgp. 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
-
construction of a strain producing Kgp proteinase without the adhesin domains in a Rgp/Kgp/adhesin-null mutant, mutant strains 33277, KDP133, and KDP137 phenotypes, overview
-
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
a naive camel nanobody library is constructed and phage display is used to select one nanobody toward RgpB with picomolar affinity. The nanobody is highly specific for RgpB given that it does not bind to the homologous gingipain HRgpA, indicating the presence of a binding epitope within the immunoglobulin-like domain of RgpB. RgpB can be used as a specific biomarker for Porphyromonas gingivalis infection
diagnostics
-
the enzyme activity is used for detection of periodontitis at an early stage of the disease
drug development
-
potential target for the development of an anti-periodontitis vaccination
medicine
molecular biology
-
enzyme is a convenient tool for protein chemistry due to its stability and activity under conditions of high detergent concentration used in protein solubilization and purification
pharmacology
medicine
-
development of structure-based inhibitors for treatment of periodontal diseases
medicine
-
development of potent, gingipain-specific inhibitors might be a helpful tool in a therapeutic strategy to prevent or treat periodontal disease
medicine
-
development of structure-based inhibitors for treatment of periodontal diseases
-
pharmacology
-
enzyme structure is an excellent template for the rational design of drugs with a potential to cure and prevent periodontitis
pharmacology
-
enzyme structure is an excellent template for the rational design of drugs with a potential to cure and prevent periodontitis
-
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