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Literature summary extracted from

  • Mistry, D.V.; Stockley, R.A.
    The cleavage specificity of an IgA1 protease from Haemophilus influenzae (2011), Virulence, 2, 103-110.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.21.72 gene iga, DNA and amino acid sequence determination and analysis Haemophilus influenzae

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.72 additional information no inhibition by natural protease inhibitors SLPI, alpha-1-antitrypsin, cathepsin G and cystatin C, and by synthetic protease inhibitors Tos-Lys-chloromethylketone, and ZD0892 Haemophilus influenzae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.21.72 human IgA1 + H2O Haemophilus influenzae unique cleavage specificity of the NTHI IgA1 protease ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.72 Haemophilus influenzae P44969 non-typeable Haemophilus influenzae, NTHI, gene iga
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.21.72 additional information NTHI is a Gram-negative coccobacillus, which colonizes the human upper respiratory tract as part of the normal flora Haemophilus influenzae
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.72 human IgA1 + H2O unique cleavage specificity of the NTHI IgA1 protease Haemophilus influenzae ?
-
 ?
3.4.21.72 human IgA1 + H2O deglycosylated human IgA1, the IgA1 protease cleaves two peptide bonds within the human IgA1 hinge region at replicate sequences, cleavage of human IgA1 produces two different sized Fc fragments with N-terminal sequence Thr-Pro-Ser-Pro-Ser Haemophilus influenzae ?
-
 ?
3.4.21.72 additional information no activity with human IgA2 Haemophilus influenzae ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.21.72 IgA1 protease
-
 Haemophilus influenzae