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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

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

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.47 gingipain K

Inhibitors

Inhibitors on EC 3.4.22.47 - gingipain K

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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-(3-phenylpropionyl)piperidine-3-(R,S)-carboxylic acid-[4-amino-1(S)-(benzothiazole-2-carbonyl)butyl] amide
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reversible inhibition
benzamidine derivatives
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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-lysyl-acyloxyketone
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benzyloxycarbonyl-L-phenylalanyl-L-lysylacyloxyketone
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the inhibitor completely abolishes osteoclastogenesis induced by Kgp
benzyloxycarbonyl-Phe-Lys-chloromethylketone
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i.e. z-FKck, specific for Kgp
carbobenzoxy-Glu(NHN(CH3)Ph)-Lys-CO-NHCH2Ph
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carbobenzoxy-Lys-Arg-CO-Lys-N-(CH3)2
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cathepsin B inhibitor
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Chlorhexidine
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synergistic effect of Zn2+ in a 1:1 ratio of chlorhexidine and Zn2+
Chloromethyl ketones
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development of diverse inhibitor derivatives: structure-based design, chemistry, and activity, specificity for the Sn binding pocket of the enzyme, overview
Chloromethylketones
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CuSO4
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1 mM, 79% inhibition
FeCl3
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1 mM, 42% inhibition
Gly-Gly
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200 mM, 50% inhibition
iodoacetamide
iodoacetic acid
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1 mM, 76% inhibition
kappa-casein
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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
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KYT-36
lactoferrin
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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
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leupeptin
lysine
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slight inhibition of coaggregation of Porphyromonas gingivalis with other oral bacteria by L-lysine and more slightly by D-lysine
MnSO4
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1 mM, 50% inhibition
N-alpha-p-tosyl-L-lysine chloromethyl ketone
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0.1 mM, complete inhibition
N-ethylmaleimide
Nalpha-benzoyl-Phe-Lys-chloromethyl ketone
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a specific inhibitor of lysine gingipain
p-hydroxymercuribenzoate
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0.2 mM, 68% inhibition
Phe-Pro-Arg-chloromethyl ketone
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0.1 mM, 95% inhibition
porcine pancreatic secretory trypsin inhibitor
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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
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Pro-Phe-Arg-chloromethylketone
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rice grain extract
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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
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tetracycline
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tosyl-L-lysine chloromethyl ketone
tosyl-L-phenylalanine chloromethyl ketone
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1 mM, 99% inhibition
tosyl-Lys-chloromethylketone
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Z-Phe-Lys-2,4,6-trimethyl-benzoyloxymethyl-ketone
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specific inhibition of Kgp
Z-Phe-Lys-acyloxymethylketone
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oxyhemoglobin-Kgp interactions resulting in formation of a hemoglobin hemichrome are inhibited by specific inhibitor Z-Phe-Lys-acyloxymethylketone
zFKck
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human gingvial epithelial cells treated with Kgp-specific inhibitor leupeptin and challenged with Porphyromonas gingivalis cells do not undergo apoptosis
ZnCl2
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1 mM, 50% inhibition
additional information
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