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Literature summary for 3.4.22.37 extracted from
- 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
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| glycylglycine | stimulates depending on the substrate | Porphyromonas gingivalis |  |
Application
| Application | Comment | Organism |
|---|---|---|
| diagnostics | the enzyme activity is used for detection of periodontitis at an early stage of the disease | Porphyromonas gingivalis |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| initial translation products, overview | Porphyromonas gingivalis |
General Stability
| General Stability | Organism |
|---|---|
| Ca2+ stabilizes all forms of gingipain R | Porphyromonas gingivalis |
| RgpB is stable to denaturing agents, e.g. urea, SDS, Triton X-100, and 1% octyl or decylpyranoside | Porphyromonas gingivalis |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| alpha2-Macroglobulin | - |
Porphyromonas gingivalis | |
| antipain | - |
Porphyromonas gingivalis | |
| D-Phe-Phe-Arg-chloromethane | irreversible, strong inhibition | Porphyromonas gingivalis | |
| D-Phe-Pro-Arg-chloromethane | irreversible, strong inhibition | Porphyromonas gingivalis | |
| doxycyclin | uncompetitive | Porphyromonas gingivalis | |
| E64 | reversible, competitive inhibition | Porphyromonas gingivalis | |
| EDTA | - |
Porphyromonas gingivalis | |
| iodoacetamide | irreversible inhibition | Porphyromonas gingivalis | |
| iodoacetic acid | irreversible inhibition | Porphyromonas gingivalis | |
| leupeptin | - |
Porphyromonas gingivalis | |
| additional information | RgpB is stable to denaturing agents, e.g. urea, SDS, Triton X-100, and 1% octyl or decylpyranoside | Porphyromonas gingivalis | |
| N-ethylmaleimide | irreversible inhibition | Porphyromonas gingivalis | |
| tetracyclin | uncompetitive | Porphyromonas gingivalis | |
| Zn2+ | - |
Porphyromonas gingivalis | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | associated to the outer membrane and vesicles | Porphyromonas gingivalis | 16020 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | stabilizes all forms of gingipain R, not necessary for activity | Porphyromonas gingivalis | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| factor IX proenzyme + H2O | Porphyromonas gingivalis | activation through limited proteolysis | ? | - |
? | |
| factor X proenzyme + H2O | Porphyromonas gingivalis | activation through limited proteolysis | ? | - |
? | |
| interferon gamma + H2O | Porphyromonas gingivalis | degradation leading to local cytokine paralysis impairing the inflammation-dependent host defense mechanisms | ? | - |
? | |
| interleukin 12 + H2O | Porphyromonas gingivalis | degradation leading to local cytokine paralysis impairing the inflammation-dependent host defense mechanisms | ? | - |
? | |
| 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 | ? | - |
? | |
| protein C + H2O | Porphyromonas gingivalis | activation through limited proteolysis | ? | - |
? | |
| prothrombin + H2O | Porphyromonas gingivalis | activation through limited proteolysis | ? | - |
? | |
| TNFalpha + H2O | Porphyromonas gingivalis | degradation leading to local cytokine paralysis impairing the inflammation-dependent host defense mechanisms | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Porphyromonas gingivalis | - |
gene rgp, RgpA and RgpB enzymes | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | - |
Porphyromonas gingivalis |
| proteolytic modification | gingipain R performs autoprocessing and activation to mature enzyme, overview | Porphyromonas gingivalis |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| 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)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Bz-L-Arg-4-nitroanilide + H2O | - |
Porphyromonas gingivalis | Bz-L-Arg + 4-nitroaniline | - |
? | |
| factor IX proenzyme + H2O | activation through limited proteolysis | Porphyromonas gingivalis | ? | - |
? | |
| factor X proenzyme + H2O | activation through limited proteolysis | Porphyromonas gingivalis | ? | - |
? | |
| interferon gamma + H2O | degradation | Porphyromonas gingivalis | ? | - |
? | |
| interferon gamma + H2O | degradation leading to local cytokine paralysis impairing the inflammation-dependent host defense mechanisms | Porphyromonas gingivalis | ? | - |
? | |
| interleukin 12 + H2O | degradation | Porphyromonas gingivalis | ? | - |
? | |
| interleukin 12 + H2O | degradation leading to local cytokine paralysis impairing the inflammation-dependent host defense mechanisms | Porphyromonas gingivalis | ? | - |
? | |
| 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 | ? | - |
? | |
| additional information | the enzyme is specific for peptide substrate with Arg at P1 position, gingipain R performs autoprocessing and activation | Porphyromonas gingivalis | ? | - |
? | |
| protein C + H2O | activation through limited proteolysis | Porphyromonas gingivalis | ? | - |
? | |
| prothrombin + H2O | activation through limited proteolysis | Porphyromonas gingivalis | ? | - |
? | |
| TNFalpha + H2O | degradation | Porphyromonas gingivalis | ? | - |
? | |
| TNFalpha + H2O | degradation leading to local cytokine paralysis impairing the inflammation-dependent host defense mechanisms | Porphyromonas gingivalis | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| 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
| Synonyms | Comment | Organism |
|---|---|---|
| More | the enzyme belongs to the peptidase family C25, clan CD | Porphyromonas gingivalis |
| RGP | - |
Porphyromonas gingivalis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 9.5 | - |
substrate Bz-L-Arg-nitroanilide | Porphyromonas gingivalis |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 9.5 | 50% of maximal activity at pH 5.0 | Porphyromonas gingivalis |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0015 | 0.0022 | E64 | - |
Porphyromonas gingivalis | |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Porphyromonas gingivalis | isoelectric focusing | 5 | 4 |
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