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Literature summary for 3.4.22.37 extracted from

  • Banbula, A.; Mak, P.; Smoluch, M.; Travis, J.; Potempa, J.
    Arginine-specific cysteine proteinase from Porphyromonas gingivalis as a convenient tool in protein chemistry (2001), Biol. Chem., 382, 1399-1404.
    View publication on PubMed
Search for more literature for 3.4.22.37

Activating Compound

Activating Compound Comment Organism Structure
dithiothreitol activates Porphyromonas gingivalis
L-cysteine activates Porphyromonas gingivalis
additional information enzyme activity and cleavage pattern are not affected by 0.1% SDS, 1% Triton X-100, or 1% octyl- and decylpyranoside Porphyromonas gingivalis
Urea 3fold activation at 6 M, probably due to unfolding of the substrate azocasein, which enhances the enzymes sensitivity for proteolytic cleavage Porphyromonas gingivalis

Application

Application Comment Organism
molecular biology enzyme is a convenient tool for protein chemistry due to its stability and activity under conditions of high detergent concentration used in protein solubilization and purification Porphyromonas gingivalis

General Stability

General Stability Organism
1% SDS slightly decreases enzyme activity Porphyromonas gingivalis
enzyme is completely inactivated in 8 M urea Porphyromonas gingivalis
RgpB is stable and active in buffers containing 6 M urea, 0.1% SDS, 1% Triton X-100, and 1% octyl or decylpyranoside Porphyromonas gingivalis

Inhibitors

Inhibitors Comment Organism Structure
additional information enzyme activity and cleavage pattern are not affected by 0.1% SDS, 1% Triton X-100, 1% octyl- and decylpyranoside Porphyromonas gingivalis

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Porphyromonas gingivalis
-
 enzyme form RgpB
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-globin + H2O absolutely specific cleavage of all Arg-Xaa peptides bonds, in presence of 4 M urea, because alpha-globin is not soluble at neutral pH Porphyromonas gingivalis ?
-
 ?
azocasein + H2O
-
 Porphyromonas gingivalis ?
-
 ?
beta-globin + H2O absolutely specific cleavage of all Arg-Xaa peptides bonds, in presence of 4 M urea, because beta-globin is not soluble at neutral pH Porphyromonas gingivalis ?
-
 ?
Lysozyme + H2O absolutely specific cleavage of all Arg-Xaa peptides bonds Porphyromonas gingivalis ?
-
 ?
protein + H2O
-
 Porphyromonas gingivalis peptides
-
 ?
ribonuclease A + H2O absolutely specific cleavage of all Arg-Xaa peptides bonds Porphyromonas gingivalis ?
-
 ?

Synonyms

Synonyms Comment Organism
Arginine-specific cysteine protease
-
 Porphyromonas gingivalis
RgpB
-
 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
7.6
-
 assay at Porphyromonas gingivalis