Information on EC 3.4.22.47 - gingipain K

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The expected taxonomic range for this enzyme is: Porphyromonas gingivalis

EC NUMBER
COMMENTARY
3.4.22.47
-
RECOMMENDED NAME
GeneOntology No.
gingipain K
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
endopeptidase with strict specificity for lysyl bonds
show the reaction diagram
-
-
-
-
endopeptidase with strict specificity for lysyl bonds
show the reaction diagram
active site structure, role of the Sn binding pocket, molecular basis for substrate specificity
-
endopeptidase with strict specificity for lysyl bonds
show the reaction diagram
active site structure, role of the Sn binding pocket, molecular basis for substrate specificity
Porphyromonas gingivalis HG66
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
gingipain K
Porphyromonas gingivalis ATCC33277
-
-
-
HbR
-
adhesin domain of gingipain which is able to bind heme as an iron nutrient source for Porphyromonas gingivalis
K-specific gingipain protease
-
-
KGP
-
gingipains are classified according to their cleavage-site specificity into Kgps, lysine-specific gingipains, and Rgps, arginine-specific gingipains
KGP
-
high molecular weight form containing both catalytic and adhesin subunit
KGP
Porphyromonas gingivalis ATCC33277, Porphyromonas gingivalis H66
-
-
-
KGP
Porphyromonas gingivalis HG66
-
gingipains are classified according to their cleavage-site specificity into Kgps, lysine-specific gingipains, and Rgps, arginine-specific gingipains
-
Lys-gingipain
-
-
-
-
Lys-gingipain
B2RLK2
-
Lys-gingipain
Porphyromonas gingivalis HG66, Porphyromonas gingivalis W83
-
-
-
Lys-specific cysteine proteinase gingipain
-
-
lysine gingipain
-
-
lysine-sepcific cysteine protease
-
-
lysine-specific gingipain
-
-
lysine-specific gingipain K
-
-
lysine-specific gingipain protease
-
-
lysine-specific gingipain proteinase
-
-
lysine-specific proteinase
-
-
PrtP proteinase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
159745-69-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
gene kgp, strain A7436
-
-
Manually annotated by BRENDA team
gene kgp, wild-type strain W50, Kgp-deficient strain K1A
-
-
Manually annotated by BRENDA team
gingipain R deficient strain KDP112
-
-
Manually annotated by BRENDA team
peridontal pathogen capable of invading aortic, heart, and human umbilical vein endothelial cells
-
-
Manually annotated by BRENDA team
strain ATCC 33277
-
-
Manually annotated by BRENDA team
strain ATCC 33277, gene kgp
-
-
Manually annotated by BRENDA team
strain ATCC33277
-
-
Manually annotated by BRENDA team
strain H66; strains ATCC33277, W50, W83 and OMGS 100
-
-
Manually annotated by BRENDA team
strains ATCC33277 and W50/ATCC 53978
-
-
Manually annotated by BRENDA team
Porphyromonas gingivalis ATCC33277
strain ATCC33277
-
-
Manually annotated by BRENDA team
Porphyromonas gingivalis H66
strain H66
-
-
Manually annotated by BRENDA team
Porphyromonas gingivalis HG66
strain HG66
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
Porphyromonas gingivalis triple mutant RgpA/RgpB/Kgp cells or the Lys-gingipain (Kgp) mutant K1A cells do not induce apoptosis in human gingvial epithelial cells
malfunction
-
the roles of several virulence factors in homotypic biofilm development by Porphyromonas gingivalis. A Kgp mutant formed markedly thick biofilms filled with large clumped colonies in PBS as well as in diluted trypticase soy broth. Autoaggregation is significantly increased in the Kgp mutants, with a clear association with alteration of biofilm structures under the non-proliferation condition. Results suggests that Kgp has a suppressive and regulatory role during biofilm development and acts coordinately with other virulence factors such as long (FimA) and short (Mfa) fimbriae to regulate the development of mature biofilms
malfunction
-
using Porphyromonas gingivalis null mutant KDP136 (triple mutant for RgpA/RgpB/Kgp) gingipain-sensitive ligand are identified. Two proteins encoded by protein-coding sequence PGN_0748 and PGN_0728 are obtained
malfunction
-
Porphyromonas gingivalis secretes outer membrane vesicles that contain major virulence factors, including Arg-gingipain and Lys-gingipain. Kgp-null membrane vesicles enter the cells and degrade transferrin receptor, while they scarcely degrade paxillin and focal adhesion kinase
malfunction
-
human keratinocyte Rgp-deficient and Kgp-deficient double mutant cells do not cleave protease-activated recptor-1 and -2. The single Kgp-negative mutant cleaves protease-activated recptor-1
metabolism
-
Porphyromonas gingivalis Lys-gingipain (Kgp) facilitates heme acquisition by HmuY (heme-binding protein)
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
-
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
-
using erythrocyte and its membrane as a model, it is shown that recombinant HbR expressed in Escherichia coli can inhibit heme-induced haemolysis, probably through removing heme from the heme-membrane complex and lowering free heme toxicity by mediating dimerization of heme molecules
physiological function
-
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
-
gingipains induce the degradation and inactivation of endothelial thrombomodulin which may promote vascular coagulation and inflammation
physiological function
-
the K2 domain of KgP induces haemolysis of erythrocytes in a dose-dependent manner that is augmented by the blocking of anion transport
physiological function
-
gingipain K is an IgG protease of pathophysiological importance
physiological function
-
results suggest that gingipains may have a role in the resistance of Porphyromonas gingivalis ATCC 49417 to human beta-defensin 3
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-lysine-4-nitroanilide + H2O
acetyl-lysine + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
acid-soluble human placental type I collagen + H2O
fragments of acid-soluble human placental type I collagen
show the reaction diagram
-
-
-
-
-
adrenocorticotropic hormone fragment 11-24 + H2O
fragments of adrenocorticotropic hormone fragment 11-24
show the reaction diagram
-
-
-
?
benzoxycarbonyl-L-lysine-4-nitroanilide + H2O
benzoxycarbonyl-L-lysine + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-L-Lys-p-nitroanilide + H2O
benzyloxycarbonyl-L-Lys + p-nitroaniline + H2O
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-L-Lys-p-nitroanilide + H2O
benzyloxycarbonyl-L-Lys + p-nitroaniline + H2O
show the reaction diagram
-
7% of activity with N-p-tosyl-Gly-Pro-Lys-p-nitroanilide
-
-
-
benzyloxycarbonyl-L-Lys-p-nitroanilide + H2O
benzyloxycarbonyl-L-Lys + p-nitroaniline + H2O
show the reaction diagram
Porphyromonas gingivalis H66
-
-
-
?
beta-endorphin + H2O
fragments of beta-endorphin
show the reaction diagram
-
-
-
?
bovine hemoglobin + H2O
fragments of bovine hemoglobin
show the reaction diagram
-
-
-
-
-
bovine serum albumin + H2O
fragments of bovine serum albumin
show the reaction diagram
-
-
-
-
-
bradykinin + H2O
fragments of bradykinin
show the reaction diagram
-
together with gingipain R, gingipain K induces vascular permeability enhancement in human plasma by cleaving bradykinin from high molecular weight kininogen
-
-
-
bradykinin + H2O
fragments of bradykinin
show the reaction diagram
-
together with gingipain R, gingipain K induces vascular permeability enhancement in human plasma by cleaving bradykinin from high molecular weight kininogen
-
?
casein + H2O
fragments of casein
show the reaction diagram
-
-
-
-
-
CBZ-Phe-Arg-4-methyl-coumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
CD46 + H2O
?
show the reaction diagram
-
recombinant CD46 is degraded by Lys-gingipain in a dose-dependent manner
-
-
?
D-Val-Leu-Lys-p-nitroanilide + H2O
D-Val-Leu-Lys + p-nitroaniline
show the reaction diagram
-
-
-
-
D-Val-Leu-Lys-p-nitroanilide + H2O
D-Val-Leu-Lys + p-nitroaniline
show the reaction diagram
Porphyromonas gingivalis, Porphyromonas gingivalis H66
-
-
-
?
D-Val-Phe-Lys-p-nitroanilide + H2O
D-Val-Phe-Lys + p-nitroaniline
show the reaction diagram
-
-
-
?
D-Val-Phe-Lys-p-nitroanilide + H2O
D-Val-Phe-Lys + p-nitroaniline
show the reaction diagram
-
70% of activity with N-p-tosyl-Gly-Pro-Lys-p-nitroanilide
-
-
D-Val-Phe-Lys-p-nitroanilide + H2O
D-Val-Phe-Lys + p-nitroaniline
show the reaction diagram
Porphyromonas gingivalis H66
-
-
-
?
elafin + H2O
?
show the reaction diagram
B2RLK2
all three gingipains have the ability to degrade elafin (endogenous inhibitor secreted by epithelial cells)
-
-
?
Fibrinogen + H2O
Fragments of fibrinogen
show the reaction diagram
-
prominent target among plasma proteins
-
?
Fibrinogen + H2O
Fragments of fibrinogen
show the reaction diagram
-
most prominent target among plasma proteins
-
-
-
focal adhesion kinase + H2O
?
show the reaction diagram
-
Kgp is responsible for degradation of integrin-related molecules
-
-
?
haptoglobin + H2O
fragments of haptoglobin
show the reaction diagram
-
human serum haptoglobin
-
?
Hemoglobin + H2O
?
show the reaction diagram
-
degradation, degradation, the enzyme forms a complex with the outer membrane receptor HmuR required for binding and utilization of hemoglobin and hemin, overview
-
-
?
hemoglobin + H2O
fragments of hemoglobin
show the reaction diagram
-
human serum hemoglobin
-
?
hemopexin + H2O
fragments of hemopexin
show the reaction diagram
-
human serum hemopexin
-
?
human beta-defensin 3 + H2O
?
show the reaction diagram
-
-
-
-
?
human IgA + H2O
cleaved human IgA
show the reaction diagram
-
-
-
-
-
human IgG + H2O
fragments of human IgG
show the reaction diagram
-
-
-
-
-
IgG1 + H2O
?
show the reaction diagram
-
The heavy chain of IgG1 is cleaved at a single site within the hinge region, generating Fab and Fc fragments
-
-
?
IgG3 + H2O
?
show the reaction diagram
-
IgG3 is cleaved within the heavy chain and at several sites around the CH2 region
-
-
?
IL-6 + H2O
fragments of IL-6
show the reaction diagram
-
-
-
?
interleukin 8 + H2O
fragments of interleukin 8
show the reaction diagram
-
-
-
-
-
interleukin 8 + H2O
fragments of interleukin 8
show the reaction diagram
-
degradation of human interleukin 8 in Porphyromonas gingivalis-infected human umbilical vein endothelial cells
-
-
-
interleukin 8 + H2O
fragments of interleukin 8
show the reaction diagram
-
degradation of human interleukin 8 in Porphyromonas gingivalis-infected human umbilical vein endothelial cells
-
?
interleukin-1beta + H2O
?
show the reaction diagram
-
low activity, biological inactivation and degradation, low activity, cytokine degradation is mainly the result of Lys-gingipain
-
-
?
interleukin-6 + H2O
?
show the reaction diagram
-
-, biological inactivation and degradation
-
-
?
interleukin-8 + H2O
?
show the reaction diagram
-
-, biological inactivation and degradation
-
-
?
melittin + H2O
fragments of melittin
show the reaction diagram
-
-
-
?
MeoSuc-Ala-Ala-Pro-Val-4-nitroanilide + H2O
?
show the reaction diagram
B2RLK2
-
-
-
?
Met-Lys-bradykinin + H2O
fragments of Met-Lys-bradykinin
show the reaction diagram
-
-
-
?
methemoglobin + H2O
?
show the reaction diagram
-
methemoglobin, formed by treatment of oxyHb with either NaNO2 or by pre-incubation with HRgpA, is rapidly degraded by Kgp compared to oxyhemoglobin
-
-
?
methemoglobin + H2O
?
show the reaction diagram
-
degradation, ligation of methemoglobin with N3-, which effectively blocks heme dissociation from the protein, prevents hemoglobin breakdown, from horse, degradation, no activity with oxyhemoglobin
-
-
?
methemoglobin + H2O
?
show the reaction diagram
Porphyromonas gingivalis HG66
-
methemoglobin, formed by treatment of oxyHb with either NaNO2 or by pre-incubation with HRgpA, is rapidly degraded by Kgp compared to oxyhemoglobin
-
-
?
monocyte chemotactic protein 1 + H2O
fragments of monocyte chemotactic protein 1
show the reaction diagram
-
degradation of human monocyte chemotactic protein 1 in Porphyromonas gingivalis-infected human umbilical vein endothelial cells
-
-
-
N-(p-tosyl)-Gly-Pro-Lys 4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
N-(p-tosyl)-Gly-Pro-Lys-4-nitroanilide + H2O
N-(p-tosyl)-Gly-Pro-Lys + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-4-tosyl-Gly-Pro-Lys-4-nitroanilide + H2O
N-4-tosyl-Gly-Pro-Lys + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-alpha-acetyl-L-lysine-4-nitroanilide + H2O
N-alpha-acetyl-L-lysine + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-alpha-acetyl-L-lysine-p-nitroanilide + H2O
N-alpha-acetyl-L-lysine + 4-nitroaniline
show the reaction diagram
-
-
-
-
r
N-alpha-benzoyl-DL-lysine 4-nitroanilide + H2O
N-alpha-benzoyl-DL-lysine + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-alpha-benzyloxycarbonyl-L-lysine-4-nitroanilide + H2O
N-alpha-benzyloxycarbonyl-L-lysine + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-p-tosyl-Gly-Pro-Lys-4-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Lys + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-p-tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Lys + p-nitroaniline
show the reaction diagram
-
-
-
-
N-p-tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Lys + p-nitroaniline
show the reaction diagram
-
-
-
-
N-p-tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Lys + p-nitroaniline
show the reaction diagram
Porphyromonas gingivalis, Porphyromonas gingivalis H66
-
gingipain K cleaves specifically on the C-terminal side of peptide substrates
-
?
Nalpha-acetyl-L-lysine 4-nitroanilide + H2O
Nalpha-acetyl-L-lysine + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
neurotensin + H2O
Glu-Leu-Tyr-Glu-Asn-Lys + Arg-Arg-Pro-Tyr-Ile-Leu
show the reaction diagram
Porphyromonas gingivalis, Porphyromonas gingivalis H66
-
-
-
?
osteoprotegerin + H2O
?
show the reaction diagram
-
degradation, digestion, enhanced osteoclastogenesis by Kgp, in co-cultures of mouse bone-marrow cells and osteoblasts, formation of multinucleated osteoclasts induced by 1alpha,25-dihydroxyvitamin D3 is augmented by Kgp. The specific enzymatic activity of Kgp is necessary for osteoclast formation, overview
-
-
?
osteoprotegerin + H2O
?
show the reaction diagram
Porphyromonas gingivalis HG66
-
degradation, digestion, enhanced osteoclastogenesis by Kgp, in co-cultures of mouse bone-marrow cells and osteoblasts, formation of multinucleated osteoclasts induced by 1alpha,25-dihydroxyvitamin D3 is augmented by Kgp. The specific enzymatic activity of Kgp is necessary for osteoclast formation, overview
-
-
?
oxyhaemoglobin + H2O
?
show the reaction diagram
-
-
-
-
?
paxillin + H2O
?
show the reaction diagram
-
Kgp is responsible for degradation of integrin-related molecules
-
-
?
protease-activated receptor-2 + H2O
?
show the reaction diagram
-
specific substrate for Lys-gingipain
-
-
?
t-butyl-oxycarbonyl-L-Glu-L-Lys-L-Lys-4-methyl-7-coumarylamide + H2O
t-butyl-oxycarbonyl-L-Glu-L-Lys-L-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
-
41% of activity with t-butyl-oxycarbonyl-L-Val-L-Leu-L-Lys-4-methyl-7-coumarylamide
-
?
t-butyl-oxycarbonyl-L-Val-L-Leu-L-Lys-4-methyl-7-coumarylamide + H2O
t-butyl-oxycarbonyl-L-Val-L-Leu-L-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
-
gingipain K has a stron preference for substrates containing Lys in the p1 site
-
?
t-butyloxycarbonyl-Val-Leu-Lys-Phe-Arg-4-methyl-7-coumarylamide
t-butyl-oxycarbonyl-Val-Leu-Lys + Phe-Arg-4-methyl-7-coumarylaminde
show the reaction diagram
-
-
-
-
?
thrombomodulin + H2O
?
show the reaction diagram
-
Lys-gingipain and Arg-gingipain cleave thrombomodulin in vitro
-
-
?
TNFalpha + H2O
?
show the reaction diagram
-
degradation, degradation, leading to inhibition of biological functions of TNFalpha, overview
-
-
?
transferrin + H2O
fragments of transferrin
show the reaction diagram
-
human serum transferrin
-
?
Val-Leu-Lys-4-nitroanilide + h2O
Val-Leu-Lys + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
monocyte chemotactic protein 1 + H2O
fragments of monocyte chemotactic protein 1
show the reaction diagram
-
degradation of human monocyte chemotactic protein 1 in Porphyromonas gingivalis-infected human umbilical vein endothelial cells
-
?
additional information
?
-
-
a combination of both arginine- and lysine-specific gingipain activity is necessary for the generation of the micro-oxo bishaem-containing pigment from haemoglobin, interaction with oxyhemoglobin, overview
-
-
-
additional information
?
-
-
gingipain K adds to gingipain R-mediated coaggregation of Porphyromonas gingivalis with other oral bacteria, it is a virulence factor, overview
-
-
-
additional information
?
-
-
gingipains are essential for bacterial virulence and survival
-
-
-
additional information
?
-
-
the C-terminal domains of the gingipain K polyprotein are necessary for assembly of the active enzyme and expression of associated activities
-
-
-
additional information
?
-
-
the enzyme degrades host iron- and heme-containing proteins, regulation of enzyme expression, overview, inhibition of gingipain increases the hmuR gene expression encoding the heme/hemoglobin receptor HmuR, and decreases the cell growth in the early and middle stages, but not in the late stages, hmuR expression inhibition decreases enzyme expression
-
-
-
additional information
?
-
-
the enzyme inactivates a cell surface ligand on Porphyromonas gingivalis that induces TLR2-and TLR4-independent signaling involving CD25, but has no effect on TLR2-and TLR4-dependent signaling, overview
-
-
-
additional information
?
-
-
role of the Sn binding pocket, molecular basis for substrate specificity, overview
-
-
-
additional information
?
-
-
extracellular gingipain protease activities cause a lack of secondary cytokine response in human cells after challenge with live Porphyromonas gingivalis
-
-
-
additional information
?
-
-
gingipains are considered to be key virulence factors of the bacterium in relation to periodontal diseases. Kgp suppresses interleukin-8 production in human HSC-2 epithelial cells requiring both the hemagglutinin and the enzymic domains. Suppression of IL-8 resultes in attenuation of the cellular recognition of bacteria, and as a consequence, sustain chronic inflammation
-
-
-
additional information
?
-
-
gingipains are cysteine proteinases and virulence factors of Porphyromonas gingivalis, the major causative bacterium of periodontal disease. Gingipains stimulate interleukin-8 secretion from human THP-1 cells, which is completely inhibited by proteinase inhibitors of gingipain and is increased in the presence of pathogen-associated molecular patterns, PAMPs. The synergism of gingipain HRgpA and PAMPs stimulates interleukin IL-6, and monocyte chemoattractant protein MCP-1 secretion, overview
-
-
-
additional information
?
-
-
gingipains are key virulence determinants of Porphyromonas gingivalis and play a crucial role in pathogenicity
-
-
-
additional information
?
-
-
gingipains reduce cyclin expression and cause early G1 arrest, leading to the inhibition of cellular proliferation in murine ST2 osteoblastic/stromal cells, overview
-
-
-
additional information
?
-
-
the membrane protein PG27, encoded by gene PG0027, is essential for the secretion of gingipains, overview
-
-
-
additional information
?
-
Porphyromonas gingivalis HG66
-
gingipains are essential for bacterial virulence and survival, role of the Sn binding pocket, molecular basis for substrate specificity, overview
-
-
-
additional information
?
-
Porphyromonas gingivalis HG66
-
gingipains are considered to be key virulence factors of the bacterium in relation to periodontal diseases. Kgp suppresses interleukin-8 production in human HSC-2 epithelial cells requiring both the hemagglutinin and the enzymic domains. Suppression of IL-8 resultes in attenuation of the cellular recognition of bacteria, and as a consequence, sustain chronic inflammation
-
-
-
additional information
?
-
Porphyromonas gingivalis ATCC33277
-
gingipains reduce cyclin expression and cause early G1 arrest, leading to the inhibition of cellular proliferation in murine ST2 osteoblastic/stromal cells, overview
-
-
-
additional information
?
-
-
the membrane protein PG27, encoded by gene PG0027, is essential for the secretion of gingipains, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
bradykinin + H2O
fragments of bradykinin
show the reaction diagram
-
together with gingipain R, gingipain K induces vascular permeability enhancement in human plasma by cleaving bradykinin from high molecular weight kininogen
-
-
-
elafin + H2O
?
show the reaction diagram
B2RLK2
all three gingipains have the ability to degrade elafin (endogenous inhibitor secreted by epithelial cells)
-
-
?
Fibrinogen + H2O
Fragments of fibrinogen
show the reaction diagram
-
most prominent target among plasma proteins
-
-
-
focal adhesion kinase + H2O
?
show the reaction diagram
-
Kgp is responsible for degradation of integrin-related molecules
-
-
?
Hemoglobin + H2O
?
show the reaction diagram
-
degradation, the enzyme forms a complex with the outer membrane receptor HmuR required for binding and utilization of hemoglobin and hemin, overview
-
-
?
interleukin 8 + H2O
fragments of interleukin 8
show the reaction diagram
-
-
-
-
-
interleukin 8 + H2O
fragments of interleukin 8
show the reaction diagram
-
degradation of human interleukin 8 in Porphyromonas gingivalis-infected human umbilical vein endothelial cells
-
-
-
interleukin-1beta + H2O
?
show the reaction diagram
-
biological inactivation and degradation, low activity, cytokine degradation is mainly the result of Lys-gingipain
-
-
?
interleukin-6 + H2O
?
show the reaction diagram
-
biological inactivation and degradation
-
-
?
interleukin-8 + H2O
?
show the reaction diagram
-
biological inactivation and degradation
-
-
?
methemoglobin + H2O
?
show the reaction diagram
-
degradation, ligation of methemoglobin with N3-, which effectively blocks heme dissociation from the protein, prevents hemoglobin breakdown
-
-
?
osteoprotegerin + H2O
?
show the reaction diagram
Porphyromonas gingivalis, Porphyromonas gingivalis HG66
-
digestion, enhanced osteoclastogenesis by Kgp, in co-cultures of mouse bone-marrow cells and osteoblasts, formation of multinucleated osteoclasts induced by 1alpha,25-dihydroxyvitamin D3 is augmented by Kgp. The specific enzymatic activity of Kgp is necessary for osteoclast formation, overview
-
-
?
paxillin + H2O
?
show the reaction diagram
-
Kgp is responsible for degradation of integrin-related molecules
-
-
?
protease-activated receptor-2 + H2O
?
show the reaction diagram
-
specific substrate for Lys-gingipain
-
-
?
TNFalpha + H2O
?
show the reaction diagram
-
degradation, leading to inhibition of biological functions of TNFalpha, overview
-
-
?
monocyte chemotactic protein 1 + H2O
fragments of monocyte chemotactic protein 1
show the reaction diagram
-
degradation of human monocyte chemotactic protein 1 in Porphyromonas gingivalis-infected human umbilical vein endothelial cells
-
-
-
additional information
?
-
-
a combination of both arginine- and lysine-specific gingipain activity is necessary for the generation of the micro-oxo bishaem-containing pigment from haemoglobin, interaction with oxyhemoglobin, overview
-
-
-
additional information
?
-
-
gingipain K adds to gingipain R-mediated coaggregation of Porphyromonas gingivalis with other oral bacteria, it is a virulence factor, overview
-
-
-
additional information
?
-
-
gingipains are essential for bacterial virulence and survival
-
-
-
additional information
?
-
-
the C-terminal domains of the gingipain K polyprotein are necessary for assembly of the active enzyme and expression of associated activities
-
-
-
additional information
?
-
-
the enzyme degrades host iron- and heme-containing proteins, regulation of enzyme expression, overview, inhibition of gingipain increases the hmuR gene expression encoding the heme/hemoglobin receptor HmuR, and decreases the cell growth in the early and middle stages, but not in the late stages, hmuR expression inhibition decreases enzyme expression
-
-
-
additional information
?
-
-
the enzyme inactivates a cell surface ligand on Porphyromonas gingivalis that induces TLR2-and TLR4-independent signaling involving CD25, but has no effect on TLR2-and TLR4-dependent signaling, overview
-
-
-
additional information
?
-
-
extracellular gingipain protease activities cause a lack of secondary cytokine response in human cells after challenge with live Porphyromonas gingivalis
-
-
-
additional information
?
-
-
gingipains are considered to be key virulence factors of the bacterium in relation to periodontal diseases. Kgp suppresses interleukin-8 production in human HSC-2 epithelial cells requiring both the hemagglutinin and the enzymic domains. Suppression of IL-8 resultes in attenuation of the cellular recognition of bacteria, and as a consequence, sustain chronic inflammation
-
-
-
additional information
?
-
-
gingipains are cysteine proteinases and virulence factors of Porphyromonas gingivalis, the major causative bacterium of periodontal disease. Gingipains stimulate interleukin-8 secretion from human THP-1 cells, which is completely inhibited by proteinase inhibitors of gingipain and is increased in the presence of pathogen-associated molecular patterns, PAMPs. The synergism of gingipain HRgpA and PAMPs stimulates interleukin IL-6, and monocyte chemoattractant protein MCP-1 secretion, overview
-
-
-
additional information
?
-
-
gingipains are key virulence determinants of Porphyromonas gingivalis and play a crucial role in pathogenicity
-
-
-
additional information
?
-
-
gingipains reduce cyclin expression and cause early G1 arrest, leading to the inhibition of cellular proliferation in murine ST2 osteoblastic/stromal cells, overview
-
-
-
additional information
?
-
-
the membrane protein PG27, encoded by gene PG0027, is essential for the secretion of gingipains, overview
-
-
-
additional information
?
-
Porphyromonas gingivalis HG66
-
gingipains are essential for bacterial virulence and survival
-
-
-
additional information
?
-
Porphyromonas gingivalis HG66
-
gingipains are considered to be key virulence factors of the bacterium in relation to periodontal diseases. Kgp suppresses interleukin-8 production in human HSC-2 epithelial cells requiring both the hemagglutinin and the enzymic domains. Suppression of IL-8 resultes in attenuation of the cellular recognition of bacteria, and as a consequence, sustain chronic inflammation
-
-
-
additional information
?
-
Porphyromonas gingivalis ATCC33277
-
gingipains reduce cyclin expression and cause early G1 arrest, leading to the inhibition of cellular proliferation in murine ST2 osteoblastic/stromal cells, overview
-
-
-
additional information
?
-
-
the membrane protein PG27, encoded by gene PG0027, is essential for the secretion of gingipains, overview
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Zn2+
-
enhances the inhibitory effect of chlorhexidine
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1-(3-phenylpropionyl)piperidine-3-(R,S)-carboxylic acid-[4-amino-1(S)-(benzothiazole-2-carbonyl)butyl] amide
-
reversible inhibition
benzamidine derivatives
-
-
benzyloxycarbonyl-L-phenylalanyl-L-lysyl-acyloxyketone
-
-
benzyloxycarbonyl-L-phenylalanyl-L-lysylacyloxyketone
-
the inhibitor completely abolishes osteoclastogenesis induced by Kgp
benzyloxycarbonyl-Phe-Lys-chloromethylketone
-
i.e. z-FKck, specific for Kgp
carbobenzoxy-Glu(NHN(CH3)Ph)-Lys-CO-NHCH2Ph
-
-
carbobenzoxy-Lys-Arg-CO-Lys-N-(CH3)2
-
-
cathepsin B inhibitor
-
-
-
Chlorhexidine
-
synergistic effect of Zn2+ in a 1:1 ratio of chlorhexidine and Zn2+
Chloromethyl ketones
-
development of diverse inhibitor derivatives: structure-based design, chemistry, and activity, specificity for the Sn binding pocket of the enzyme, overview
Chloromethylketones
-
-
CuSO4
-
1 mM, 79% inhibition
FeCl3
-
1 mM, 42% inhibition
Gly-Gly
-
200 mM, 50% inhibition
iodoacetamide
-
10 mM, complete inhibition
iodoacetamide
-
1 mM, 92% inhibition
iodoacetic acid
-
1 mM, 76% inhibition
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
-
KYT-36
-
specific inhibition of Kgp, slightly inhibits coaggregation of Porphyromonas gingivalis with other bacteria in vivo
KYT-36
-
specific Kgp inhibitor
KYT-36
-
specific inhibitor for Kgp
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
-
Leupeptin
-
0.43 mM, 83% inhibition
Leupeptin
-
inhibits Arg-specific Rgp, but not Lys-specific Kgp
lysine
-
slight inhibition of coaggregation of Porphyromonas gingivalis with other oral bacteria by L-lysine and more slightly by D-lysine
N-alpha-p-tosyl-L-lysine chloromethyl ketone
-
0.1 mM, complete inhibition
N-ethylmaleimide
-
10 mM, complete inhibition
N-ethylmaleimide
-
2 mM, 65% inhibition
Nalpha-benzoyl-Phe-Lys-chloromethyl ketone
-
a specific inhibitor of lysine gingipain
p-hydroxymercuribenzoate
-
0.2 mM, 68% inhibition
Phe-Pro-Arg-chloromethyl ketone
-
0.1 mM, 95% inhibition
porcine pancreatic secretory trypsin inhibitor
-
i.e. PSTI porcine, a Kazal-type serine proteinase inhibitor purified from pancreas, porcine pancreatic secretory trypsin inhibitor having an essential Lys residue at the P1 position of the reactive site, and containing Tyr and Asn residues the P2' and P3' sites, specifically inhibits the activity of the Lys-specific gingipain K, whereas bovine inhibitor, possessing a Arg residue at the P1 position, exhibits activity only against the Arg-specific cysteine proteinase gingipain K, EC 3.4.22.37. The association equilibrium constant is 0.51 mM
-
Pro-Phe-Arg-chloromethylketone
-
-
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
-
tosyl-L-lysine chloromethyl ketone
-
1 mM, 96% inhibition
tosyl-L-lysine chloromethyl ketone
-
0.05 mM, 81% inhibition
tosyl-L-lysine chloromethyl ketone
-
-
tosyl-L-phenylalanine chloromethyl ketone
-
1 mM, 99% inhibition
tosyl-Lys-chloromethylketone
-
-
Z-Phe-Lys-2,4,6-trimethyl-benzoyloxymethyl-ketone
-
specific inhibition of Kgp
Z-Phe-Lys-acyloxymethylketone
-
oxyhemoglobin-Kgp interactions resulting in formation of a hemoglobin hemichrome are inhibited by specific inhibitor Z-Phe-Lys-acyloxymethylketone
zFKck
-
human gingvial epithelial cells treated with Kgp-specific inhibitor leupeptin and challenged with Porphyromonas gingivalis cells do not undergo apoptosis
ZnCl2
-
1 mM, 50% inhibition
MnSO4
-
1 mM, 50% inhibition
additional information
-
gingipains stimulate interleukin-8 secretion from human THP-1 cells, which is completely inhibited by proteinase inhibitors of gingipain and is increased in the presence of pathogen-associated molecular patterns, PAMPs, overview
-
additional information
-
in the gene PG0027, encoding protein PG27, deletion mutant 83K10, the activities of Arg-gingipain and Lys-gingipain are severely reduced, while the activities of secreted exopeptidases DPPIV, DPP-7, and PTP-A are unaffected
-
additional information
-
no inhibition by chicken ovoinhibitor III and IV domains
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
-
2-mercaptoethanol
-
30 mM, 197% increase in activity
cysteine
-
most effective reducing agent for activation, maximal activation at 50 mM
cysteine
-
3 mM, 166% increase in activity
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 37C for 10 min
dithiothreitol
-
30 mM, 315% increase in activity
EDTA
-
2 mM, 79% increase in activity
EGTA
-
2 mM, 79% increase in activity
additional information
-
gingipains stimulate interleukin-8 secretion from human THP-1 cells, which is completely inhibited by proteinase inhibitors of gingipain and is increased in the presence of pathogen-associated molecular patterns, PAMPs, overview
-
additional information
-
membrane protein PG27 is essential for secretion of gingipains and their extracellular activity, and is localized in both the inner and outer membranes
-
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
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.18
-
benzyloxycarbonyl-L-Lys-p-nitroanilide
-
pH 8.5, 37C
0.2
-
D-Val-Leu-Lys-p-nitroanilide
-
pH 8.5, 37C
0.126
-
D-Val-Phe-Lys-p-nitroanilide
-
pH 8.5, 37C
0.05
-
N-p-tosyl-Gly-Pro-Lys-p-nitroanilide
-
pH 8.5, 37C
0.0029
-
Hemoglobin
-
pH 7.6, 37C, human serum hemoglobin
-
additional information
-
additional information
-
gingipain K binds hemoglobin, porphyrins and metalloporphyrins
-
additional information
-
additional information
-
Investigation of the enzyme kinetics of IgG proteolysis by gingipain K, using FPLC- and isothermal titration calorimetry-based assays followed by Hill plots, reveal non-Michaelis-Menten kinetics involving a mechanism of positive cooperativity
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
9.4
-
Hemoglobin
-
pH 7.6, 37C, human serum hemoglobin
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
9e-07
-
1-(3-phenylpropionyl)piperidine-3-(R,S)-carboxylic acid-[4-amino-1(S)-(benzothiazole-2-carbonyl)butyl]amide
-
-
additional information
-
additional information
-
inhibition kinetics, overview
-
additional information
-
additional information
-
inhibition kinetics
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.26
-
-
substrate N-p-tosyl-Gly-Pro-Lys-p-nitroanilide
0.356
-
-
release of 7-amino-4-methylcoumarin
additional information
-
-
enzyme activity and hemoglobin/hemin binding in wild-type strain A7436 and in kgp-deficient mutant strains WS1, WS10, and WS15, overview
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
-
hydrolysis of t-butyloxycarbonyl-L-Val-L-Leu-L-Lys-4-methyl-7-coumarylamide
7.6
8.3
-
assay at
8
-
-
hydrolysis of small synthetic peptides
8
-
-
coaggregation assay at
8
-
B2RLK2
assay at
8.5
-
-
with protein substrates like azocasein
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
9.5
-
hydrolysis of t-butyl-oxycarbonyl-L-Val-L-Leu-L-Lys-4-methyl-7-coumarylamide
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
coaggregation assay at room temperature
22
-
-
assay at room temperature
37
-
B2RLK2
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Porphyromonas gingivalis HG66
-
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Porphyromonas gingivalis HG66
-
; the enzyme is secreted
-
-
Manually annotated by BRENDA team
-
the enzyme is secreted
-
-
Manually annotated by BRENDA team
-
outer membrane associated
Manually annotated by BRENDA team
-
outer membrane protein Sov paticipates in the secretion of Lys-gingipain
Manually annotated by BRENDA team
-
Porphyromonas gingivalis secretes outer membrane vesicles that contain major virulence factors, including Arg-gingipain and Lys-gingipain
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50000
-
-
SDS-PAGE
52000
-
-
gel filtration
105000
-
-
gel filtration without boiling
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 105000, gingipain K-hemagglutinin complex, enzyme exists in multiple forms, SDS-PAGE; x * 60000, catalytic domain of gingipain K, immunoblot
?
-
x * 80000, gelatin-containing SDS-PAGE
?
-
x * 60000, SDS-PAGE
?
-
x * 48000, SDS-PAGE
?
-
x * 105000, SDS-PAGE
?
Porphyromonas gingivalis H66
-
x * 105000, gingipain K-hemagglutinin complex, enzyme exists in multiple forms, SDS-PAGE; x * 60000, catalytic domain of gingipain K, immunoblot; x * 60000, SDS-PAGE
-
?
Porphyromonas gingivalis HG66
-
x * 105000, SDS-PAGE
-
monomer
-
1 * 51000, SDS-PAGE
additional information
-
the predominant form of gingipain K is a complex of the 60000 Da catalytic domain with hemagglutinins, enzyme is build of a prepropeptide, a catalytic domain and a hemagglutinin domain
additional information
-
structure homology modeling
additional information
-
the enzyme is expressed as a large precursor protein consisting of a leader sequence, a pro-fragment, a catalytic domain with a C-terminal IgG-like subdomain, and a large hemagglutinin/adhesion domain, the latter is required for proper enzyme folding
additional information
Porphyromonas gingivalis HG66
-
structure homology modeling
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
proteolytic modification
P72197
gingipain K is synthesized as a polyprotein precursor that contains a proteinase domain and multiple adhesin domains, this precursor is processed at distinct sites to yield active KGP
proteolytic modification
-
the enzyme is expressed as a large precursor protein consisting of a leader sequence, a pro-fragment, a catalytic domain with a C-terminal IgG-like subdomain, and a large hemagglutinin/adhesion domain, the enzyme cleaves itself autocatalytically
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the crystal structure of a domain within the haemagglutinin region of Kgp is reported here. The K2 domain structure is a jellyroll fold with two anti-parallel beta-sheets. This fold topology is shared with adhesive domains from functionally diverse receptors such as MAM domains, ephrin receptor ligand binding domains and a number of carbohydrate binding modules
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.5
-
-
40% loss of activity after 5 min
5
9
-
stable for several hours in the absence of cysteine, rapid loss of activity below pH 8.0 in the presence of cysteine
5.5
10.5
-
0C, no loss of activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
no loss of activity
37
-
-
no loss of activity
45
-
-
no loss of activity after 2 h
45
-
-
68% loss of activity after 10 min, 97% loss of activity after 30 min
60
-
-
rapid inactivation
60
-
-
60% loss of activity after 10 min
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Kgp shows a loss of only 1% and 8% of initial activity after 7 and 24 h, respectively
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
acetone precipitate, Sephadex G-150, arginine-Sepharose
-
ammonium sulfate, immunoaffinity column, Mono S
-
ammonium sulfate, Mono Q, chromatofocusing on MonoP
-
Lys-gingipain is purified from the cell envelope extract of Porphyromonas gingivalis KDP112 by affinity chromatography on arginine Sepharose 4B
-
native extracellular enzyme from culture medium
-
native Kgp from culture supernatant
-
native Lys-gingipain from cell culture supernatant, re-activation of the proteases by reducing the active-centre thiol group partially oxidized during the purification process
-
purified by using gel-filtration and arginine-Sepharose chromatography
-
using gel-filtration
-
using Ni-NTA chromatography and gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Sf9 insect cells
P72197
expression of wild-type and mutant enzymes in murine ST2 osteoblastic/stromal cells
-
HbR domain is recombinantly expressed in Escherichia coli
-
the gene fragment encoding the K2 domain (Ala1157-Gly1334) of Kgp from Porphyromonas gingivalis W83 is cloned into a modified vector pET-32a. The constructed plasmid is transformed into Escherichia coli BL21(DE3) competent cells for protein expression
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C476A
-
high Kgp activity and black pigmentation
C476A/C477A
-
no Kgp activity nor black pigmentation
C477A
-
no Kgp activity nor black pigmentation
additional information
-
construction of kgp-deficient mutant strains WS1, WS10, and WS15, and of Kgp and HmuR double mutants, which show reduced hemoglobin degradation and utilization due to abolished enzyme activity, Arg-specific gingipain R, EC 3.4.22.37, can compensate partially for the mutation, overview
additional information
-
strain K1A is Kgp-deficient
additional information
-
kgp-deficient mutant strain WS10 shows 22 fold increased hmuR expression, while the kgp expression is decreased in the hmuR-deficient mutant strain WS1
additional information
-
construction of several C-terminally truncated enzyme mutant strains, which show decreased activity compared to the wild-type strain as well as altered distribution of the enzyme between membrane-associated and secreted forms, overview
additional information
-
the results indicate that the Cys477 residue is essential for both the Kgp activity and the black pigmentation of Porphyromonas gingivalis
additional information
-
complement killing resistancy of Porphyromonas gingivalis is examined using Arg- and Lys-gingipain (K1A) deletion mutants and polysaccharide synthesis deletion mutants. Arg- and Lys-gingipain (K1A) deletion mutants maintained resistance to killing
additional information
-
strains: Rgp/Kgp-null (rgpA rgpB kgpdeficient) triple-mutant KDP136 and the Kgp-null mutant (KDP129)
additional information
-
UV-visible spectroscopy is used to examine the interaction of iron(III) protoporphyrin IX monomers [Fe(III)PPIX.OH] with recombinant HA2 and purified HRgpA, Kgp and RgpB gingipains.The HA2 domain of Kgp reacts with Fe(III)PPIX.OH to form micro-oxo bishaem, the presence of which is confirmed by Fourier transform infrared spectroscopy. Both HRgpA and Kgp, but not RgpB, also mediate micro-oxo bishaem formation and aggregation
additional information
-
in the gene PG0027, encoding protein PG27, deletion mutant 83K10, the activities of Arg-gingipain and Lys-gingipain are severely reduced, while the activities of secreted exopeptidases DPPIV, DPP-7, and PTP-A are unaffected
additional information
-
construction of a strain producing Kgp proteinase without the adhesin domains in a Rgp/Kgp/adhesin-null mutant, mutant strains 33277, KDP133, and KDP160 phenotypes, overview
additional information
-
construction of enzyme-deficient mutants KDP136 with DELTArgpADELTArgpBDELTAkgp, and KDP129 with DELTArgpADELTArgpB. The mutants do not, in contrast to the wild-type enzyme, inhibit cellular proliferation and don not arrest the cell cycle in the G0/G1 phase as well as decrease the expression levels of the cell-cycle regulatory molecules cyclin D and cyclin E in murine ST2 cells, overview
additional information
-
gingipain-deficient Porphyromonas gingivalis mutants lacking both Arg- and Lys-gingipains are unable to induce interleukin-1beta, interleukin-6, and interleukin-8 degradation
additional information
Porphyromonas gingivalis ATCC33277
-
construction of enzyme-deficient mutants KDP136 with DELTArgpADELTArgpBDELTAkgp, and KDP129 with DELTArgpADELTArgpB. The mutants do not, in contrast to the wild-type enzyme, inhibit cellular proliferation and don not arrest the cell cycle in the G0/G1 phase as well as decrease the expression levels of the cell-cycle regulatory molecules cyclin D and cyclin E in murine ST2 cells, overview
-
additional information
Porphyromonas gingivalis HG66
-
construction of a strain producing Kgp proteinase without the adhesin domains in a Rgp/Kgp/adhesin-null mutant, mutant strains 33277, KDP133, and KDP160 phenotypes, overview
-
additional information
-
in the gene PG0027, encoding protein PG27, deletion mutant 83K10, the activities of Arg-gingipain and Lys-gingipain are severely reduced, while the activities of secreted exopeptidases DPPIV, DPP-7, and PTP-A are unaffected
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
development of structure-based inhibitors for treatment of periodontal diseases
medicine
-
results indicate that degradation of apoB-100 by Rgp but not Kgp plays a crucial role in the promotion of atherosclerosis by Porphyromonas gingivalis infection
medicine
-
development of potent, gingipain-specific inhibitors might be a helpful tool in a therapeutic strategy to prevent or treat periodontal disease
molecular biology
-
a combination of both R- and K-gingipains is required for pigment production from oxyhemoglobin by Porphyromonas gingivalis since R-gingipain converts oxyhemoglobin into the methemoglobin form which is more susceptible to Kgp degradation for the eventual release of iron(III) protoporphyrin IX and production of the micro-oxo haem dimer
molecular biology
-
it is shown that the production of anionic polysaccharide at the surface of Porphyromonas gingivalis rather than Arg- and Lys-gingipain synthesis is the principal mechanism of serum resistance in Porphyromonas gingivalis
medicine
Porphyromonas gingivalis HG66
-
development of structure-based inhibitors for treatment of periodontal diseases
-
molecular biology
Porphyromonas gingivalis HG66
-
a combination of both R- and K-gingipains is required for pigment production from oxyhemoglobin by Porphyromonas gingivalis since R-gingipain converts oxyhemoglobin into the methemoglobin form which is more susceptible to Kgp degradation for the eventual release of iron(III) protoporphyrin IX and production of the micro-oxo haem dimer
-