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Literature summary for 3.4.22.37 extracted from

  • Toh, E.C.; Dashper, S.G.; Huq, N.L.; Attard, T.J.; OBrien-Simpson, N.M.; Chen, Y.Y.; Cross, K.J.; Stanton, D.P.; Paolini, R.A.; Reynolds, E.C.
    Porphyromonas gingivalis cysteine proteinase inhibition by kappa-casein peptides (2011), Antimicrob. Agents Chemother., 55, 1155-1161.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.37

Inhibitors

Inhibitors Comment Organism Structure
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 Porphyromonas gingivalis

Organism

Organism UniProt Comment Textmining
Porphyromonas gingivalis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Nalpha-benzoyl-L-Arg-4-nitroanilide + H2O
-
 Porphyromonas gingivalis Nalpha-benzoyl-L-Arg + 4-nitroaniline
-
 ?

Synonyms

Synonyms Comment Organism
RgpA
-
 Porphyromonas gingivalis
RgpB
-
 Porphyromonas gingivalis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Porphyromonas gingivalis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Porphyromonas gingivalis