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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additional information
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distribution of igaB among clinical isolates of nontypeable Haemophilus influenzae, overview
additional information
NTHI is a Gram-negative coccobacillus, which colonizes the human upper respiratory tract as part of the normal flora
additional information
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NTHI is a Gram-negative coccobacillus, which colonizes the human upper respiratory tract as part of the normal flora
additional information
bacterial isolates show wide variability in IgA1 protease activity, and those isolated from patients with clinical infection possess the highest levels of activity, overview
additional information
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bacterial isolates show wide variability in IgA1 protease activity, and those isolated from patients with clinical infection possess the highest levels of activity, overview