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Literature summary for 3.4.22.37 extracted from

  • Potempa, J.; Mikolajczyk-Pawlinska, J.; Brassell, D.; Nelson, D.; Thogersen, I.B.; Enghild, J.J.; Travis, J.
    Comparative properties of two cysteine proteinases (gingipains R), the products of two related but individual genes of Porphyromonas gingivalis (1998), J. Biol. Chem., 273, 21648-21657.
    View publication on PubMed
Search for more literature for 3.4.22.37

Activating Compound

Activating Compound Comment Organism Structure
2-mercaptoethanol weak activation, a concentration above 100 mM is required Porphyromonas gingivalis
cysteamine activates, best above 5 mM Porphyromonas gingivalis
cysteine 10 mM, most effective reducing agent for activation of the enzyme, denaturation occurs at higher concentration above 5 mM Porphyromonas gingivalis
dithiothreitol weak activation, a concentration above 100 mM is required Porphyromonas gingivalis
glutathione activates, best above 5 mM Porphyromonas gingivalis
glycyl-glycine stimulates the amidolytic activity and limited proteolysis, but destabilizes the enzyme Porphyromonas gingivalis
glycyl-glycine stimulates the amidolytic activity and limited proteolysis, but destabilizes the isozymes Porphyromonas gingivalis

General Stability

General Stability Organism
Ca2+ stabilizes the enzyme, while glycyl-glycine destabilizes the enzyme Porphyromonas gingivalis
Ca2+ stabilizes the isozymes, while glycyl-glycine destabilizes the isozymes Porphyromonas gingivalis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Porphyromonas gingivalis

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular secretion Porphyromonas gingivalis
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ stabilizes the activity Porphyromonas gingivalis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
48120 48150 mature, C-terminally truncated isozymes, amino acid sequence calculation and mass spectroscopy Porphyromonas gingivalis
48120 48150 mature, C-terminally truncated isozymes, amino acid sequence calculation, gel filtration and mass spectroscopy Porphyromonas gingivalis
95000
-
 a complex of catalytic and hemagglutinin/adhesin domains, gel filtration Porphyromonas gingivalis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
protein + H2O Porphyromonas gingivalis
-
 peptides
-
 ?
protein + H2O Porphyromonas gingivalis HG66
-
 peptides
-
 ?

Organism

Organism UniProt Comment Textmining
Porphyromonas gingivalis
-
 gene rgp-1, enzyme gingipain R1
-
Porphyromonas gingivalis B2RKU0 strain ATCC33277, gene rgpB gene, enzyme gingipain R2, 4 isoforms I-IV that are indistinguishable with regard to stability, pH-optima, kinetic characteristics and proteolytic activity
-
Porphyromonas gingivalis Q51844 gene rgpB/rgp-2 gene, enzyme gingipain R2, 4 isoforms I-IV that are indistinguishable with regard to stability, pH-optima, kinetic characteristics and proteolytic activity
-
Porphyromonas gingivalis ATCC 33277 B2RKU0 strain ATCC33277, gene rgpB gene, enzyme gingipain R2, 4 isoforms I-IV that are indistinguishable with regard to stability, pH-optima, kinetic characteristics and proteolytic activity
-
Porphyromonas gingivalis HG66
-
 gene rgp-1, enzyme gingipain R1
-
Porphyromonas gingivalis HG66 Q51844 gene rgpB/rgp-2 gene, enzyme gingipain R2, 4 isoforms I-IV that are indistinguishable with regard to stability, pH-optima, kinetic characteristics and proteolytic activity
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the mature enzyme is C-terminally truncated to 433 amino acid residues Porphyromonas gingivalis

Purification (Commentary)

Purification (Comment) Organism
from cell culture medium Porphyromonas gingivalis
isozymes I-IV from cell culture medium, 4.5-5fold Porphyromonas gingivalis

Reaction

Reaction Comment Organism Reaction ID
hydrolysis of proteins and small molecule substrates, with a preference for Arg in P1 proteolysis of selected proteins Porphyromonas gingivalis
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
40.8
-
 purified isozyme IV Porphyromonas gingivalis
41.3
-
 purified isozyme I Porphyromonas gingivalis
42.9
-
 purified isozyme III Porphyromonas gingivalis
45.5
-
 purified isozyme II Porphyromonas gingivalis

Storage Stability

Storage Stability Organism
-20°C, buffer with neutral pH, 1-5 mM CaCl2, indefinitely stable Porphyromonas gingivalis
0°C, on ice, buffer with neutral pH, 1-5 mM CaCl2, stable for months Porphyromonas gingivalis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha1-Antichymotrypsin + H2O inactivation of the substrate Porphyromonas gingivalis ?
-
 ?
alpha1-Antichymotrypsin + H2O inactivation of the substrate Porphyromonas gingivalis HG66 ?
-
 ?
azocasein + H2O synthetic chromogenic substrate Porphyromonas gingivalis ?
-
 ?
azocasein + H2O synthetic chromogenic substrate Porphyromonas gingivalis HG66 ?
-
 ?
benzoyl-L-arginine-4-nitroanilide + H2O synthetic fluorogenic substrate Porphyromonas gingivalis benzoyl-L-arginine + 4-nitroaniline
-
 ?
denatured alpha1-proteinase inhibitor + H2O
-
 Porphyromonas gingivalis ?
-
 ?
denatured type I collagen + H2O
-
 Porphyromonas gingivalis ?
-
 ?
denatured type I collagen + H2O
-
 Porphyromonas gingivalis HG66 ?
-
 ?
Leu-Tyr-Arg-4-nitroanilide + H2O synthetic fluorogenic substrate Porphyromonas gingivalis Leu-Tyr-Arg + 4-nitroaniline
-
 ?
additional information substrate specificity, no inactivation of native alpha1-proteinase inhibitor and native type I collagen Porphyromonas gingivalis ?
-
 ?
additional information substrate specificity, no inactivation of native alpha1-proteinase inhibitor and native type I collagen Porphyromonas gingivalis HG66 ?
-
 ?
protein + H2O
-
 Porphyromonas gingivalis peptides
-
 ?
protein + H2O
-
 Porphyromonas gingivalis HG66 peptides
-
 ?
tosyl-GPR-4-nitroanilide + H2O other substrates with a Ps proline are very poor substrates, synthetic fluorogenic substrate Porphyromonas gingivalis tosyl-GPR + 4-nitroaniline
-
 ?
Z-Arg-Arg-4-nitroanilide + H2O synthetic fluorogenic substrate Porphyromonas gingivalis Z-Arg-Arg + 4-nitroaniline
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 48019-48369, gingipain R2 isozymes I-IV and laser mass spectroscopy Porphyromonas gingivalis
monomer 1 * 48019-48369, gingipain R2 isozymes I-IV, laser mass spectroscopy Porphyromonas gingivalis
More the enzyme complex consists of 4 major polypeptides of 49.5 kDa for the catalytic domain, 43 kDa, 23.3 kDa, and 15.9 kDa Porphyromonas gingivalis

Synonyms

Synonyms Comment Organism
arginine-specific cysteine proteinase
-
 Porphyromonas gingivalis
gingipain R2 two different enzymes gingipain R exist in Porphyromonas gingivalis, that are encoded by related but individual genes Porphyromonas gingivalis
RGP-2
-
 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
7.5
-
 protein substrates Porphyromonas gingivalis
8
-
 4-nitroanilide substrates Porphyromonas gingivalis
9.5
-
 protein substrates Porphyromonas gingivalis

pH Range

pH Minimum pH Maximum Comment Organism
5 9.5 50% activity at pH 5.0, maximal activity at pH 9.5 Porphyromonas gingivalis

pI Value

Organism Comment pI Value Maximum pI Value
Porphyromonas gingivalis isoelectric focusing
-
 3.74
Porphyromonas gingivalis isozyme IV, isoelectric focusing
-
 4.96
Porphyromonas gingivalis isozyme III, isoelectric focusing
-
 5.03
Porphyromonas gingivalis isozyme II, isoelectric focusing
-
 5.09
Porphyromonas gingivalis isozyme I, isoelectric focusing
-
 5.21