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Literature summary extracted from

  • Mistry, D.; Stockley, R.A.
    IgA1 protease (2006), Int. J. Biochem. Cell Biol., 38, 1244-1248.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.4.21.72 agriculture the beta domain of the IgA1 protease is able to transport alternative proteins to the protease domain of IgA1 protease as N terminal passenger proteins. This technology has been applied to immobilised heavy metals in soil Haemophilus influenzae
3.4.21.72 agriculture the beta domain of the IgA1 protease is able to transport alternative proteins to the protease domain of IgA1 protease as N terminal passenger proteins. This technology has been applied to immobilised heavy metals in soil Neisseria gonorrhoeae
3.4.21.72 agriculture the beta domain of the IgA1 protease is able to transport alternative proteins to the protease domain of IgA1 protease as N terminal passenger proteins. This technology has been applied to immobilised heavy metals in soil Neisseria meningitidis
3.4.21.72 agriculture the beta domain of the IgA1 protease is able to transport alternative proteins to the protease domain of IgA1 protease as N terminal passenger proteins. This technology has been applied to immobilised heavy metals in soil Streptococcus pneumoniae
3.4.21.72 drug development a fusion protein of the beta domain and a single-chain antibody to transmissible gastroenteritis coronavirus has been expressed on the surface of Escherichia coli. The single-chain antibody is then able to target and block the virus from infecting epithelial cells Haemophilus influenzae
3.4.21.72 drug development a fusion protein of the beta domain and a single-chain antibody to transmissible gastroenteritis coronavirus has been expressed on the surface of Escherichia coli. The single-chain antibody is then able to target and block the virus from infecting epithelial cells Neisseria gonorrhoeae
3.4.21.72 drug development a fusion protein of the beta domain and a single-chain antibody to transmissible gastroenteritis coronavirus has been expressed on the surface of Escherichia coli. The single-chain antibody is then able to target and block the virus from infecting epithelial cells Neisseria meningitidis
3.4.21.72 drug development a fusion protein of the beta domain and a single-chain antibody to transmissible gastroenteritis coronavirus has been expressed on the surface of Escherichia coli. The single-chain antibody is then able to target and block the virus from infecting epithelial cells Streptococcus pneumoniae
3.4.21.72 medicine inactivation of the enzyme has the potential to reduce bacterial colonisation at mucosal surrfaces Haemophilus influenzae
3.4.21.72 medicine inactivation of the enzyme has the potential to reduce bacterial colonisation at mucosal surrfaces Neisseria gonorrhoeae
3.4.21.72 medicine inactivation of the enzyme has the potential to reduce bacterial colonisation at mucosal surrfaces Neisseria meningitidis
3.4.21.72 medicine inactivation of the enzyme has the potential to reduce bacterial colonisation at mucosal surrfaces Streptococcus pneumoniae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.21.72 cell membrane
-
 Haemophilus influenzae
-
-
3.4.21.72 cell membrane
-
 Neisseria gonorrhoeae
-
-
3.4.21.72 cell membrane
-
 Neisseria meningitidis
-
-
3.4.21.72 cell membrane
-
 Streptococcus pneumoniae
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.21.72 IgA1 + H2O Haemophilus influenzae
-
 ?
-
 ?
3.4.21.72 IgA1 + H2O Neisseria gonorrhoeae
-
 ?
-
 ?
3.4.21.72 IgA1 + H2O Neisseria meningitidis
-
 ?
-
 ?
3.4.21.72 IgA1 + H2O Streptococcus pneumoniae
-
 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.72 Haemophilus influenzae
-
-
-
3.4.21.72 Neisseria gonorrhoeae
-
-
-
3.4.21.72 Neisseria meningitidis
-
-
-
3.4.21.72 Streptococcus pneumoniae
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.72 IgA1 + H2O
-
 Haemophilus influenzae ?
-
 ?
3.4.21.72 IgA1 + H2O
-
 Neisseria gonorrhoeae ?
-
 ?
3.4.21.72 IgA1 + H2O
-
 Neisseria meningitidis ?
-
 ?
3.4.21.72 IgA1 + H2O
-
 Streptococcus pneumoniae ?
-
 ?
3.4.21.72 additional information in vitro studies show that the enzyme also cleaves human chorionic gonadotrophin hormone, granulocyte-macrophage colony stimulating factor, the CD8 surface antigen of cytotoxic T lymphocytes and LAMP 1 a membrane glycoprotein of lysosomes Haemophilus influenzae ?
-
 ?
3.4.21.72 additional information in vitro studies showed that the enzyme also cleaves human chorionic gonadotrophin hormone, granulocyte-macrophage colony stimulating factor, the CD8 surface antigen of cytotoxic T lymphocytes and LAMP 1 a membrane glycoprotein of lysosomes Neisseria gonorrhoeae ?
-
 ?
3.4.21.72 additional information in vitro studies showed that the enzyme also cleaves human chorionic gonadotrophin hormone, granulocyte-macrophage colony stimulating factor, the CD8 surface antigen of cytotoxic T lymphocytes and LAMP 1 a membrane glycoprotein of lysosomes Neisseria meningitidis ?
-
 ?
3.4.21.72 additional information in vitro studies showed that the enzyme also cleaves human chorionic gonadotrophin hormone, granulocyte-macrophage colony stimulating factor, the CD8 surface antigen of cytotoxic T lymphocytes and LAMP 1 a membrane glycoprotein of lysosomes Streptococcus pneumoniae ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.21.72 IgA1 protease
-
 Haemophilus influenzae
3.4.21.72 IgA1 protease
-
 Neisseria gonorrhoeae
3.4.21.72 IgA1 protease
-
 Neisseria meningitidis
3.4.21.72 IgA1 protease
-
 Streptococcus pneumoniae