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Literature summary for 3.4.22.47 extracted from

  • Vincents, B.; Guentsch, A.; Kostolowska, D.; von Pawel-Rammingen, U.; Eick, S.; Potempa, J.; Abrahamson, M.
    Cleavage of IgG1 and IgG3 by gingipain K from Porphyromonas gingivalis may compromise host defense in progressive periodontitis (2011), FASEB J., 25, 3741-3750.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.47

KM Value [mM]

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

Organism UniProt Comment Textmining
Porphyromonas gingivalis
-
-
-

Substrates and Products (Substrate)

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

Synonyms Comment Organism
gingipain K
-
 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
8
-
 assay at Porphyromonas gingivalis

General Information

General Information Comment Organism
physiological function gingipain K is an IgG protease of pathophysiological importance Porphyromonas gingivalis