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 |
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 |
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 | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.21.72 | Haemophilus influenzae | - |
- |
- |
3.4.21.72 | Haemophilus influenzae ATCC 49247 | - |
- |
- |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
3.4.21.72 | proteolytic modification | the enzyme performs autocatalysis at its autocleavage site | Haemophilus influenzae |
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 |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|
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 | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.4.21.72 | IgA protease | - |
Haemophilus influenzae |
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 |