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Literature summary for 3.4.22.47 extracted from

  • Taiyoji, M.; Shitomi, Y.; Taniguchi, M.; Saitoh, E.; Ohtsubo, S.
    Identification of proteinaceous inhibitors of a cysteine proteinase (an Arg-specific gingipain) from Porphyromonas gingivalis in rice grain, using targeted-proteomics approaches (2009), J. Proteome Res., 8, 5165-5174.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
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 Porphyromonas gingivalis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
SDS-PAGE Porphyromonas gingivalis

Organism

Organism UniProt Comment Textmining
Porphyromonas gingivalis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CBZ-Phe-Arg-4-methyl-coumaryl-7-amide + H2O
-
Porphyromonas gingivalis ?
-
?

Synonyms

Synonyms Comment Organism
KGP
-
Porphyromonas gingivalis
Lys-gingipain
-
Porphyromonas gingivalis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
assay at Porphyromonas gingivalis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Porphyromonas gingivalis