3.4.22.47: gingipain K
This is an abbreviated version!
For detailed information about gingipain K, go to the full flat file.
Word Map on EC 3.4.22.47
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3.4.22.47
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gingivalis
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porphyromonas
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periodontal
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gingipains
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arg-gingipains
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proteinases
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arginine-specific
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crevicular
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keystone
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hrgpa
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subgingival
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molecular biology
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black-pigmented
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gingivalis-induced
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coaggregation
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medicine
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arg-specific
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gingipain-deficient
- 3.4.22.47
- gingivalis
- porphyromonas
- periodontal
-
gingipains
- arg-gingipains
- proteinases
-
arginine-specific
-
crevicular
-
keystone
- hrgpa
-
subgingival
- molecular biology
-
black-pigmented
-
gingivalis-induced
-
coaggregation
- medicine
-
arg-specific
-
gingipain-deficient
Reaction
endopeptidase with strict specificity for lysyl bonds =
Synonyms
gingipain, gingipain K, HbR, K-gingipain, K-specific gingipain protease, KGP, Lys-gingipain, 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, porphypain, PrtP proteinase
ECTree
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General Information
General Information on EC 3.4.22.47 - gingipain K
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malfunction
metabolism
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Porphyromonas gingivalis Lys-gingipain (Kgp) facilitates heme acquisition by HmuY (heme-binding protein)
physiological function
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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 Kgp-negative mutant cleaves protease-activated recptor-1
malfunction
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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
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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
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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
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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
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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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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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gingipains induce the degradation and inactivation of endothelial thrombomodulin which may promote vascular coagulation and inflammation
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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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
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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
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gingipain K is an IgG protease of pathophysiological importance
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