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Literature summary for 3.4.21.72 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
Search for more literature for 3.4.21.72

Cloned(Commentary)

Cloned (Comment) Organism
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]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
130000
-
 recombinant extracellular His6-tagged IgA protease, gel filtration Haemophilus influenzae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
immunglobulin A1 + H2O Haemophilus influenzae human IgA1, cleavage at the hinge region immunglobulin Fc + immunglobulin Fd
-
 ?
immunglobulin A1 + H2O Haemophilus influenzae ATCC 49247 human IgA1, cleavage at the hinge region immunglobulin Fc + immunglobulin Fd
-
 ?
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 ?
-
 ?
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

Organism UniProt Comment Textmining
Haemophilus influenzae
-
-
-
Haemophilus influenzae ATCC 49247
-
-
-

Posttranslational Modification

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

Purification (Commentary)

Purification (Comment) Organism
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

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
immunglobulin A1 + H2O human IgA1, cleavage at the hinge region Haemophilus influenzae immunglobulin Fc + immunglobulin Fd
-
 ?
immunglobulin A1 + H2O human IgA1, cleavage at the hinge region Haemophilus influenzae ATCC 49247 immunglobulin Fc + immunglobulin Fd
-
 ?
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 ?
-
 ?
additional information the enzyme performs autocatalysis at its autocleavage site Haemophilus influenzae ?
-
 ?
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 ?
-
 ?
additional information the enzyme performs autocatalysis at its autocleavage site Haemophilus influenzae ATCC 49247 ?
-
 ?

Synonyms

Synonyms Comment Organism
IgA protease
-
 Haemophilus influenzae

General Information

General Information Comment Organism
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
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