3.4.21.72: IgA-specific serine endopeptidase
This is an abbreviated version!
For detailed information about IgA-specific serine endopeptidase, go to the full flat file.
Word Map on EC 3.4.21.72
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3.4.21.72
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neisseria
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haemophilus
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streptococcus
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influenzae
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gonorrhoeae
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hinge
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meningitidis
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sanguis
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autotransporter
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pneumococcal
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gonococcal
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serogroups
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meningococci
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oralis
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medicine
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protease-producing
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lactamica
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nontypeable
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paraproteins
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ramosum
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enzyme-neutralizing
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urealyticum
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pharmacology
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agriculture
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drug development
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analysis
- 3.4.21.72
- neisseria
- haemophilus
- streptococcus
- influenzae
- gonorrhoeae
- hinge
- meningitidis
- sanguis
-
autotransporter
- pneumococcal
-
gonococcal
-
serogroups
-
meningococci
- oralis
- medicine
-
protease-producing
- lactamica
-
nontypeable
-
paraproteins
- ramosum
-
enzyme-neutralizing
- urealyticum
- pharmacology
- agriculture
- drug development
- analysis
Reaction
Cleavage of immunoglobulin A molecules at certain Pro-/- bonds in the hinge region. No small molecule substrates are known =
Synonyms
Iga, IgA protease, IgA protease A1, IgA protease B2, IgA proteinase, IgA-specific proteinase, IgA1 protease, IgA1-protease, IgA1-specific protease, IgA1?P, IgA1P, IgA1pr, IgaA1, IgaA2, IgaB2, IgAP, Immunoglobulin A protease, Immunoglobulin A proteinase, immunoglobulin A1 protease, NMB IgA1 protease, Proteinase, immunoglobulin A, serine-type IgA1 protease, serine-type immunoglobulin A1 protease, ST-11 IgA protease, type 2 IgA1 protease
ECTree
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Posttranslational Modification
Posttranslational Modification on EC 3.4.21.72 - IgA-specific serine endopeptidase
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proteolytic modification
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the enzyme performs autocatalysis at its autocleavage site
proteolytic modification
Haemophilus influenzae ATCC 49247
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the enzyme performs autocatalysis at its autocleavage site
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proteolytic modification
self-cleavage is required for secretion of the mature extracellular enzyme form, cleavage targets contain a proline-rich consensus recognition sequence, Pro-Pro-Ser-Pro, residing in the variable linker region that connects the protease and translocator domains, the precise amino acid sequence of the intervening region, between mature IgA1 protease and the beta-core translocator domain, influences the efficiency of autoproteolytic processing
proteolytic modification
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the enzyme performs autocatalysis at its autocleavage site. Proteolytic cleavage of IgA protease may occur at two cleavage sites in ST-11 isolates LNP19995: CS1 autocleavage site (separating the protease domain from the alpha peptide) and CS2 autocleavage site (separating the alpha peptide from the translocator domain). The proteolytic cleavage may occur at the unique CS1 site, leading to release of alpha-peptide-lacking IgA protease in non-ST-11 isolates