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Literature summary for 3.4.22.10 extracted from

  • Sumitomo, T.; Nakata, M.; Higashino, M.; Terao, Y.; Kawabata, S.
    Group A streptococcal cysteine protease cleaves epithelial junctions and contributes to bacterial translocation (2013), J. Biol. Chem., 288, 13317-13324.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.10

Organism

Organism UniProt Comment Textmining
Streptococcus pyogenes
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
casein + H2O
-
 Streptococcus pyogenes ?
-
 ?
E-cadherin + H2O
-
 Streptococcus pyogenes ?
-
 ?
occludin + H2O
-
 Streptococcus pyogenes ?
-
 ?

Synonyms

Synonyms Comment Organism
SpeB
-
 Streptococcus pyogenes
streptococcal pyrogenic exotoxin B
-
 Streptococcus pyogenes

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Streptococcus pyogenes

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
 assay at Streptococcus pyogenes

General Information

General Information Comment Organism
malfunction wild type strain efficiently translocates across the epithelial monolayer along with cleavage of occludin and E-cadherin. Deletion of the speB gene compromises those activities. Destabilization of the junctional proteins is relieved in cells infected with the speB mutant, as compared with those infected with the wild type Streptococcus pyogenes