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Literature summary extracted from

  • Imamura, T.; Potempa, J.; Travis, J.
    Gingipain R (2004), Handbook of Proteolytic Enzymes (Barrett, A. J. ; Rawlings, N. D. ; Woessner, J. F. ; eds. ), 2, 1319-1328.
No PubMed abstract available

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.22.37 glycylglycine stimulates depending on the substrate Porphyromonas gingivalis

Application

EC Number Application Comment Organism
3.4.22.37 diagnostics the enzyme activity is used for detection of periodontitis at an early stage of the disease Porphyromonas gingivalis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.22.37 initial translation products, overview Porphyromonas gingivalis

General Stability

EC Number General Stability Organism
3.4.22.37 Ca2+ stabilizes all forms of gingipain R Porphyromonas gingivalis
3.4.22.37 RgpB is stable to denaturing agents, e.g. urea, SDS, Triton X-100, and 1% octyl or decylpyranoside Porphyromonas gingivalis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.22.37 alpha2-Macroglobulin
-
 Porphyromonas gingivalis
3.4.22.37 antipain
-
 Porphyromonas gingivalis
3.4.22.37 D-Phe-Phe-Arg-chloromethane irreversible, strong inhibition Porphyromonas gingivalis
3.4.22.37 D-Phe-Pro-Arg-chloromethane irreversible, strong inhibition Porphyromonas gingivalis
3.4.22.37 doxycyclin uncompetitive Porphyromonas gingivalis
3.4.22.37 E64 reversible, competitive inhibition Porphyromonas gingivalis
3.4.22.37 EDTA
-
 Porphyromonas gingivalis
3.4.22.37 iodoacetamide irreversible inhibition Porphyromonas gingivalis
3.4.22.37 iodoacetic acid irreversible inhibition Porphyromonas gingivalis
3.4.22.37 leupeptin
-
 Porphyromonas gingivalis
3.4.22.37 additional information RgpB is stable to denaturing agents, e.g. urea, SDS, Triton X-100, and 1% octyl or decylpyranoside Porphyromonas gingivalis
3.4.22.37 N-ethylmaleimide irreversible inhibition Porphyromonas gingivalis
3.4.22.37 tetracyclin uncompetitive Porphyromonas gingivalis
3.4.22.37 Zn2+
-
 Porphyromonas gingivalis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.22.37 membrane associated to the outer membrane and vesicles Porphyromonas gingivalis 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.22.37 Ca2+ stabilizes all forms of gingipain R, not necessary for activity Porphyromonas gingivalis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.22.37 factor IX proenzyme + H2O Porphyromonas gingivalis activation through limited proteolysis ?
-
 ?
3.4.22.37 factor X proenzyme + H2O Porphyromonas gingivalis activation through limited proteolysis ?
-
 ?
3.4.22.37 interferon gamma + H2O Porphyromonas gingivalis degradation leading to local cytokine paralysis impairing the inflammation-dependent host defense mechanisms ?
-
 ?
3.4.22.37 interleukin 12 + H2O Porphyromonas gingivalis degradation leading to local cytokine paralysis impairing the inflammation-dependent host defense mechanisms ?
-
 ?
3.4.22.37 additional information Porphyromonas gingivalis gingipains R are potent permeability enhancement factors by prekallikrein activation and bradykinin induction, the enzyme degrades proteins of connective tissue, cell surface proteins and receptors, cytokines and plasma proteins, including components of the coagulation and complement cascades, heme- and iron-binding proteins, immunoglobulins and proteinase inhibitors ?
-
 ?
3.4.22.37 protein C + H2O Porphyromonas gingivalis activation through limited proteolysis ?
-
 ?
3.4.22.37 prothrombin + H2O Porphyromonas gingivalis activation through limited proteolysis ?
-
 ?
3.4.22.37 TNFalpha + H2O Porphyromonas gingivalis degradation leading to local cytokine paralysis impairing the inflammation-dependent host defense mechanisms ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.22.37 Porphyromonas gingivalis
-
 gene rgp, RgpA and RgpB enzymes
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.22.37 glycoprotein
-
 Porphyromonas gingivalis
3.4.22.37 proteolytic modification gingipain R performs autoprocessing and activation to mature enzyme, overview Porphyromonas gingivalis

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.22.37 native enzyme from envelope and/or outer membranes by ammonium sulfate or acetone precipitation, ion exchange chromatography, gel filtration, isoelectric or chromatofocusing, and affinity chromatography Porphyromonas gingivalis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.22.37 Bz-L-Arg-4-nitroanilide + H2O
-
 Porphyromonas gingivalis Bz-L-Arg + 4-nitroaniline
-
 ?
3.4.22.37 factor IX proenzyme + H2O activation through limited proteolysis Porphyromonas gingivalis ?
-
 ?
3.4.22.37 factor X proenzyme + H2O activation through limited proteolysis Porphyromonas gingivalis ?
-
 ?
3.4.22.37 interferon gamma + H2O degradation Porphyromonas gingivalis ?
-
 ?
3.4.22.37 interferon gamma + H2O degradation leading to local cytokine paralysis impairing the inflammation-dependent host defense mechanisms Porphyromonas gingivalis ?
-
 ?
3.4.22.37 interleukin 12 + H2O degradation Porphyromonas gingivalis ?
-
 ?
3.4.22.37 interleukin 12 + H2O degradation leading to local cytokine paralysis impairing the inflammation-dependent host defense mechanisms Porphyromonas gingivalis ?
-
 ?
3.4.22.37 additional information gingipains R are potent permeability enhancement factors by prekallikrein activation and bradykinin induction, the enzyme degrades proteins of connective tissue, cell surface proteins and receptors, cytokines and plasma proteins, including components of the coagulation and complement cascades, heme- and iron-binding proteins, immunoglobulins and proteinase inhibitors Porphyromonas gingivalis ?
-
 ?
3.4.22.37 additional information the enzyme is specific for peptide substrate with Arg at P1 position, gingipain R performs autoprocessing and activation Porphyromonas gingivalis ?
-
 ?
3.4.22.37 protein C + H2O activation through limited proteolysis Porphyromonas gingivalis ?
-
 ?
3.4.22.37 prothrombin + H2O activation through limited proteolysis Porphyromonas gingivalis ?
-
 ?
3.4.22.37 TNFalpha + H2O degradation Porphyromonas gingivalis ?
-
 ?
3.4.22.37 TNFalpha + H2O degradation leading to local cytokine paralysis impairing the inflammation-dependent host defense mechanisms Porphyromonas gingivalis ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.22.37 More structure analysis, gingipain R occurs in different forms of 50-110 kDa, tertiary structure, the C-terminus shows an IgSF-like fold, overview Porphyromonas gingivalis

Synonyms

EC Number Synonyms Comment Organism
3.4.22.37 More the enzyme belongs to the peptidase family C25, clan CD Porphyromonas gingivalis
3.4.22.37 RGP
-
 Porphyromonas gingivalis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.22.37 9.5
-
 substrate Bz-L-Arg-nitroanilide Porphyromonas gingivalis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.22.37 5 9.5 50% of maximal activity at pH 5.0 Porphyromonas gingivalis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.4.22.37 0.0015 0.0022 E64
-
 Porphyromonas gingivalis

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.4.22.37 Porphyromonas gingivalis isoelectric focusing 5 4