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Literature summary for 3.4.22.37 extracted from

  • Imamura, T.; Banbula, A.; Pereira, P.J.B.; TRavis, J.; Potempa, J.
    Activation of human prothrombin by arginine-specific cysteine proteinases (gingipain R) from POrphyromonas gingivalis (2001), J. Biol. Chem., 276, 18984-18991.
    View publication on PubMed
Search for more literature for 3.4.22.37

Activating Compound

Activating Compound Comment Organism Structure
Phospholipids activation of prothrombin cleavage in presence of Ca2+ by HRgpA not RgpB, 1.5fold at 0.04 mg/ml Porphyromonas gingivalis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00026
-
 prothrombin HRgpA, pH 7.6, 37°C, in presence of Ca2+ and phospholipids Porphyromonas gingivalis
0.0066
-
 prothrombin RgpB, pH 7.6, 37°C, in presence of Ca2+ and phospholipids Porphyromonas gingivalis

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activation of prothrombin cleavage in presence of phospholipids by HRgpA not RgpB Porphyromonas gingivalis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
prothrombin + H2O Porphyromonas gingivalis HRgpA, involved in fibrinogen clotting thrombin + ?
-
 ?

Organism

Organism UniProt Comment Textmining
Porphyromonas gingivalis
-
 purified 95 kDa HRgpA and 50 kDa RgpB enzyme forms
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Porphyromonas gingivalis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-thrombin + H2O HRgpA and RgpB, cleavage of peptide bond R383-N394 Porphyromonas gingivalis beta-thrombin B-1 and B-2 chains
-
 ?
beta-thrombin B-2 chain + H2O HRgpA and RgpB, substrate inactivation and degradation Porphyromonas gingivalis ?
-
 ?
prothrombin + H2O HRgpA, involved in fibrinogen clotting Porphyromonas gingivalis thrombin + ?
-
 ?
prothrombin + H2O major cleavage sites of HRgpA are R271-T272, R320-I321, and R155-S156, activation of human substrate, HRgpA possesses adhesion domains and is about 20fold more active than the single chain RgpB Porphyromonas gingivalis alpha-thrombin + 2 peptide fragments high amount od alpha-thrombin ?
prothrombin + H2O major cleavage sites of RgpB are R155-S156 and R271-T272, while the peptide bond R320-I321 is not efficiently cleaved resulting in about 20fold slower reaction, activation of human substrate, less active than HRgpA Porphyromonas gingivalis alpha-thrombin + prethrombin 1 + prethrombin 2 + 1 peptide fragments low amount of alpha-thrombin ?

Synonyms

Synonyms Comment Organism
Arginine-specific cysteine protease
-
 Porphyromonas gingivalis
HRgpA
-
 Porphyromonas gingivalis
RgpB
-
 Porphyromonas gingivalis

Temperature Optimum [°C]

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.076
-
 prothrombin RgpB, pH 7.6, 37°C, in presence of Ca2+ and phospholipids Porphyromonas gingivalis
0.32
-
 prothrombin HRgpA, pH 7.6, 37°C, in presence of Ca2+ and phospholipids Porphyromonas gingivalis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
 assay at Porphyromonas gingivalis