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Literature summary extracted from

  • Wang, H.; Zhong, X.; Li, J.; Zhu, M.; Wang, L.; Ji, X.; Fan, J.; Wang, L.
    Cloning and expression of H. influenzae 49247 IgA protease in E. coli (2018), Mol. Biotechnol., 60, 134-140 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.21.72 gene igaA, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, constitutive recombinant expression of codon-optimized gene encoding His6-tagged IgA protease in Escherichia coli and secretion of the enzyme to the culture medium Haemophilus influenzae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.21.72 130000
-
recombinant extracellular His6-tagged IgA protease, gel filtration 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 immunglobulin A1 + H2O Haemophilus influenzae human IgA1, cleavage at the hinge region immunglobulin Fc + immunglobulin Fd
-
?
3.4.21.72 immunglobulin A1 + H2O Haemophilus influenzae ATCC 49247 human IgA1, cleavage at the hinge region immunglobulin Fc + immunglobulin Fd
-
?
3.4.21.72 additional information Haemophilus influenzae the IgA protease from Haemophilus influenzae strain ATCC 49247 has a high activity and the ability to degrade human in vivo deposited aberrantly glycosylated IgA1-containing immune complex ?
-
?
3.4.21.72 additional information Haemophilus influenzae ATCC 49247 the IgA protease from Haemophilus influenzae strain ATCC 49247 has a high activity and the ability to degrade human in vivo deposited aberrantly glycosylated IgA1-containing immune complex ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.72 Haemophilus influenzae
-
-
-
3.4.21.72 Haemophilus influenzae ATCC 49247
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.21.72 proteolytic modification the enzyme performs autocatalysis at its autocleavage site Haemophilus influenzae

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.21.72 recombinant extracellular His6-tagged IgA protease from Escherichia coli culture medium by nickel affinity chromatography, dialysis, and ultrafiltration, to over 95% purity Haemophilus influenzae

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.72 immunglobulin A1 + H2O human IgA1, cleavage at the hinge region Haemophilus influenzae immunglobulin Fc + immunglobulin Fd
-
?
3.4.21.72 immunglobulin A1 + H2O human IgA1, cleavage at the hinge region Haemophilus influenzae ATCC 49247 immunglobulin Fc + immunglobulin Fd
-
?
3.4.21.72 additional information the IgA protease from Haemophilus influenzae strain ATCC 49247 has a high activity and the ability to degrade human in vivo deposited aberrantly glycosylated IgA1-containing immune complex Haemophilus influenzae ?
-
?
3.4.21.72 additional information the enzyme performs autocatalysis at its autocleavage site Haemophilus influenzae ?
-
?
3.4.21.72 additional information the IgA protease from Haemophilus influenzae strain ATCC 49247 has a high activity and the ability to degrade human in vivo deposited aberrantly glycosylated IgA1-containing immune complex Haemophilus influenzae ATCC 49247 ?
-
?
3.4.21.72 additional information the enzyme performs autocatalysis at its autocleavage site Haemophilus influenzae ATCC 49247 ?
-
?

Synonyms

EC Number Synonyms Comment Organism
3.4.21.72 IgA protease
-
Haemophilus influenzae

General Information

EC Number General Information Comment Organism
3.4.21.72 evolution Haemophilus influenzae 49247 IgA protease shows unique DNA and amino acid sequence but with typical endopeptidase domain and beta transporter domain compared to known IgA proteases from the same species Haemophilus influenzae
3.4.21.72 physiological function the IgA protease from Haemophilus influenzae strain ATCC 49247 has a high activity and the ability to degrade human in vivo deposited aberrantly glycosylated IgA1-containing immune complex. In addition to be a pathogenic factor, IgA protease is also proven to serve as a potential therapeutic agent in the treatment of IgA nephropathy (IgAN) Haemophilus influenzae