EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
3.4.22.37 | dithiothreitol | activates | Porphyromonas gingivalis | |
3.4.22.37 | L-cysteine | activates | Porphyromonas gingivalis | |
3.4.22.37 | 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 | |
3.4.22.37 | Urea | 3fold activation at 6 M, probably due to unfolding of the substrate azocasein, which enhances the enzymes sensitivity for proteolytic cleavage | Porphyromonas gingivalis |
EC Number | Application | Comment | Organism |
---|---|---|---|
3.4.22.37 | 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 |
EC Number | General Stability | Organism |
---|---|---|
3.4.22.37 | 1% SDS slightly decreases enzyme activity | Porphyromonas gingivalis |
3.4.22.37 | enzyme is completely inactivated in 8 M urea | Porphyromonas gingivalis |
3.4.22.37 | 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 |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.4.22.37 | additional information | enzyme activity and cleavage pattern are not affected by 0.1% SDS, 1% Triton X-100, 1% octyl- and decylpyranoside | Porphyromonas gingivalis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.22.37 | protein + H2O | Porphyromonas gingivalis | - |
peptides | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.22.37 | Porphyromonas gingivalis | - |
enzyme form RgpB | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.22.37 | 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 | ? | - |
? | |
3.4.22.37 | azocasein + H2O | - |
Porphyromonas gingivalis | ? | - |
? | |
3.4.22.37 | 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 | ? | - |
? | |
3.4.22.37 | Lysozyme + H2O | absolutely specific cleavage of all Arg-Xaa peptides bonds | Porphyromonas gingivalis | ? | - |
? | |
3.4.22.37 | protein + H2O | - |
Porphyromonas gingivalis | peptides | - |
? | |
3.4.22.37 | ribonuclease A + H2O | absolutely specific cleavage of all Arg-Xaa peptides bonds | Porphyromonas gingivalis | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.4.22.37 | Arginine-specific cysteine protease | - |
Porphyromonas gingivalis |
3.4.22.37 | RgpB | - |
Porphyromonas gingivalis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.4.22.37 | 37 | - |
assay at | Porphyromonas gingivalis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.4.22.37 | 7.6 | - |
assay at | Porphyromonas gingivalis |