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
3.4.21.72 IgA-specific serine endopeptidaseAdvanced search results
results (
results (Engineering
Engineering on EC 3.4.21.72 - IgA-specific serine endopeptidase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
P1004A/S1005T/P1006A
site-directed mutagenesis, mutation of the cleavage recognition sequence residues
P1006X
site-directed mutagenesis, mutation of a cleavage recognition sequence residue, the mutant is still able for self-cleavage and subsequent extracellular release of mature IgA1 protease
S1005E
site-directed mutagenesis, mutation of a cleavage recognition sequence residue, the mutant is still able for self-cleavage and subsequent extracellular release of mature IgA1 protease
S267V
site-directed mutagenesis, mutation of the active site catalytic residue, inactive mutant, no self-cleavage and thus no secretion of the enzyme
S267A
additional information
S267A
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site-directed mutagenesis, catalytically inactive mutant
S267A
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site-directed mutagenesis, catalytically inactive mutant
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additional information
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construction of igaB mutants and igaA/igaB double mutants of strain 11P6H
additional information
construction of deletion or point mutants lacking the previously defined consensus cleavage site, the mutants are still able for self-cleavage and subsequent extracellular release of mature IgA1 protease
additional information
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construction of deletion or point mutants lacking the previously defined consensus cleavage site, the mutants are still able for self-cleavage and subsequent extracellular release of mature IgA1 protease
additional information
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creation of four producer strains with effective expression of recombinant proteins (in the form of inclusion bodies) that represent variants of IgA1pr from Neisseria meningitidis serogroup B (strain B44/76) with different primary structures carrying C-terminal histidine label (-LEH6). Protein I is enzymatically active IgA1pr containing M1K2-N963 sequence. Protein IIa (MA28-N963) also possessing specific enzymatic activity is a variant of protein I lacking signal peptide (M1K2-A27). Enzymatically inactive protein IIm is a variant of protein IIa with catalytically active Ser267 residue substituted with an Ala residue. Protein III, a low-molecular-weight fragment of IgA1pr (ME135-H328), is enzymatically inactive and contains a sequence in the IgA1pr region with high density of potential T- and B-cell epitopes
additional information
Neisseria meningitidis serogroup B B44/76
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creation of four producer strains with effective expression of recombinant proteins (in the form of inclusion bodies) that represent variants of IgA1pr from Neisseria meningitidis serogroup B (strain B44/76) with different primary structures carrying C-terminal histidine label (-LEH6). Protein I is enzymatically active IgA1pr containing M1K2-N963 sequence. Protein IIa (MA28-N963) also possessing specific enzymatic activity is a variant of protein I lacking signal peptide (M1K2-A27). Enzymatically inactive protein IIm is a variant of protein IIa with catalytically active Ser267 residue substituted with an Ala residue. Protein III, a low-molecular-weight fragment of IgA1pr (ME135-H328), is enzymatically inactive and contains a sequence in the IgA1pr region with high density of potential T- and B-cell epitopes
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additional information
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generation of an isogenic iga knockout mutant strain, analysis of infection efficiency and persistence in infected cells
additional information
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construction of an isogenic iga mutant DELTAiga by allelic replacement, which shows significantly decreased lethality to pigs. Removal of gene iga contributes to weakening the ability of Streptoccocus suis in breaking through the mucosa barrier of a host and its inability to invade the pigs
additional information
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construction of an isogenic iga mutant DELTAiga by allelic replacement, which shows significantly decreased lethality to pigs. Removal of gene iga contributes to weakening the ability of Streptoccocus suis in breaking through the mucosa barrier of a host and its inability to invade the pigs
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