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Literature summary for 3.4.24.13 extracted from

  • Senior, B.W.; Woof, J.M.
    Sites in the CH3 domain of human IgA1 that influence sensitivity to bacterial IgA1 proteases (2006), J. Immunol., 177, 3913-3919.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Haemophilus influenzae
-
type 2 enzyme
-
Neisseria gonorrhoeae
-
type 1 and type 2 enzyme
-
Neisseria meningitidis
-
type 1 and type 2 enzyme
-
Streptococcus mitis
-
type 1 and type 2 enzyme
-
Streptococcus oralis
-
type 1 and type 2 enzyme
-
Streptococcus pneumoniae
-
type 1 and type 2 enzyme
-
Streptococcus sanguinis
-
type 1 and type 2 enzyme
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
human IgA1 with CH3 domain exchanged for that of human IgG1 + H2O
-
Streptococcus pneumoniae ?
-
?
human IgA1 with CH3 domain exchanged for that of human IgG1 + H2O
-
Streptococcus sanguinis ?
-
?
human IgA1 with CH3 domain exchanged for that of human IgG1 + H2O
-
Streptococcus mitis ?
-
?
human IgA1 with CH3 domain exchanged for that of human IgG1 + H2O
-
Streptococcus oralis ?
-
?
additional information no substrate: human IgA1 with CH3 domain exchanged for that of human IgG1 Neisseria gonorrhoeae ?
-
?
additional information no substrate: human IgA1 with CH3 domain exchanged for that of human IgG1 Neisseria meningitidis ?
-
?
additional information no substrate: human IgA1 with CH3 domain exchanged for that of human IgG1. CH3 domain residues E403, Q406, T409 influence sensitivity to cleavage by enzyme Haemophilus influenzae ?
-
?