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
-
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
- 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
Advanced search results
Inhibitors
Inhibitors on EC 3.4.22.47 - gingipain K
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
1-(3-phenylpropionyl)piperidine-3-(R,S)-carboxylic acid-[4-amino-1(S)-(benzothiazole-2-carbonyl)butyl] amide
-
reversible inhibition
benzyl-N-[(2S)-1-[[(3S)-7-amino-1-(benzylamino)-1,2-dioxoheptan-3-yl]amino]-5-(2-methyl-2-phenylhydrazinyl)-1,5-dioxopentan-2-yl]carbamate
i.e. KYT-36, peptide-derived, potent, bioavailable and highly selective inhibitor
benzyloxycarbonyl-L-phenylalanyl-L-lysylacyloxyketone
-
the inhibitor completely abolishes osteoclastogenesis induced by Kgp
benzyloxycarbonyl-Phe-Lys-chloromethylketone
-
i.e. z-FKck, specific for Kgp
Chlorhexidine
-
synergistic effect of Zn2+ in a 1:1 ratio of chlorhexidine and Zn2+
Chloromethyl ketones
-
development of diverse inhibitor derivatives: structure-based design, chemistry, and activity, specificity for the Sn binding pocket of the enzyme, overview
kappa-casein
-
inhibits proteolytic activity associated with Porphyromonas gingivalis whole cells, purified RgpA-Kgp proteinase-adhesin complexes, and purified RgpB proteinase. The peptide kappa-casein(109-137) exhibits synergism with Zn(II) against both Arg- and Lys-specific proteinases. Active region for inhibition is identified as kappa-casein (117-137). Kappa-casein inhibits in an uncompetitive manner
-
lactoferrin
-
inhibits both the Arg- and Lys-specific proteinase activities of Porphyromonas gingivalis whole cells by approximately 40% at 1 mg/ml and over 70% at 10 mg/ml. Lactoferrin inhibits both the Arg-specific and Lys-specific activities of purified Porphyromonas gingivalis 248 RgpA/Kgp proteinase-adhesin complexes by 96% at a concentration of 5 mg/mL
-
lysine
-
slight inhibition of coaggregation of Porphyromonas gingivalis with other oral bacteria by L-lysine and more slightly by D-lysine
N-alpha-p-tosyl-L-lysine chloromethyl ketone
-
0.1 mM, complete inhibition
Nalpha-benzoyl-Phe-Lys-chloromethyl ketone
-
a specific inhibitor of lysine gingipain
porcine pancreatic secretory trypsin inhibitor
-
i.e. PSTI porcine, a Kazal-type serine proteinase inhibitor purified from pancreas, porcine pancreatic secretory trypsin inhibitor having an essential Lys residue at the P1 position of the reactive site, and containing Tyr and Asn residues the P2' and P3' sites, specifically inhibits the activity of the Lys-specific gingipain K, whereas bovine inhibitor, possessing a Arg residue at the P1 position, exhibits activity only against the Arg-specific cysteine proteinase gingipain K, EC 3.4.22.37. The association equilibrium constant is 0.51 mM
-
rice grain extract
-
a rice protein fraction is shown to have Rgp inhibitory activities. Comprehensive affinity chromatography and MS analyses results in the identification of 4 proteins a 26 kDa globulin, a plant lipid transfer/trypsin-alpha amylase inhibitor, the RA17 seed allergen, and an alpha amylase/trypsin inhibitor proteins accounting for 90% of the inhibitory activity. Inhibitory activity against Rgp is 20fold higher than that against Kgp
-
Z-Phe-Lys-2,4,6-trimethyl-benzoyloxymethyl-ketone
-
specific inhibition of Kgp
Z-Phe-Lys-acyloxymethylketone
-
oxyhemoglobin-Kgp interactions resulting in formation of a hemoglobin hemichrome are inhibited by specific inhibitor Z-Phe-Lys-acyloxymethylketone
zFKck
-
human gingvial epithelial cells treated with Kgp-specific inhibitor leupeptin and challenged with Porphyromonas gingivalis cells do not undergo apoptosis
-
specific inhibition of Kgp, slightly inhibits coaggregation of Porphyromonas gingivalis with other bacteria in vivo
-
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
-