KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Investigation of the enzyme kinetics of IgG proteolysis by gingipain K, using FPLC- and isothermal titration calorimetry-based assays followed by Hill plots, reveal non-Michaelis-Menten kinetics involving a mechanism of positive cooperativity | Porphyromonas gingivalis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Porphyromonas gingivalis | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
IgG1 + H2O | The heavy chain of IgG1 is cleaved at a single site within the hinge region, generating Fab and Fc fragments | Porphyromonas gingivalis | ? | - |
? | |
IgG3 + H2O | IgG3 is cleaved within the heavy chain and at several sites around the CH2 region | Porphyromonas gingivalis | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
gingipain K | - |
Porphyromonas gingivalis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Porphyromonas gingivalis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Porphyromonas gingivalis |
General Information | Comment | Organism |
---|---|---|
physiological function | gingipain K is an IgG protease of pathophysiological importance | Porphyromonas gingivalis |