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Information on EC 3.4.21.72 - IgA-specific serine endopeptidase
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3.4.21.72 IgA-specific serine endopeptidaseSpecify your search results
Word Map
- 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
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
iga1 protease, iga protease, immunoglobulin a1 protease, iga1p, type 2 iga1 protease, iga1-protease, immunoglobulin a protease, iga proteinase, iga1-specific protease, igaa1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IgA protease
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-
-
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IgA proteinase
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-
-
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IgA-specific proteinase
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-
-
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IgA1 protease
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-
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Immunoglobulin A protease
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-
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Immunoglobulin A proteinase
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Proteinase, immunoglobulin A
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-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cleavage of immunoglobulin A molecules at certain Pro-/- bonds in the hinge region. No small molecule substrates are known
the catalytic serine residue is Ser267
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
-
-
CAS REGISTRY NUMBER
COMMENTARY
55127-02-1
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
human immunoglobulin A1 + H2O
?
bacterial isolates show wide variability in IgA1 protease activity, and those isolated from patients with clinical infection possess the highest levels of activity, overview
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-
?
human immunoglobulin A1 + H2O
?
site-specific proteolytic cleavage
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-
?
additional information
?
-
the NMB IgA1 protease shows a broad substrate specificity for human proteins
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-
?
additional information
?
-
-
the NMB IgA1 protease shows a broad substrate specificity for human proteins
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
human immunoglobulin A1 + H2O
?
bacterial isolates show wide variability in IgA1 protease activity, and those isolated from patients with clinical infection possess the highest levels of activity, overview
-
-
?
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
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
-
bacterial isolates show wide variability in IgA1 protease activity, and those isolated from patients with clinical infection possess the highest levels of activity, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
active mature enzyme, the cleaved and maturated protein is secreted
-
inactive pro-enzyme, the cleaved and maturated protein is secreted
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
additional information
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
-
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene iga, DNA and amino acid sequence determination and analysis of NMB IgA1 protease, sequence comparisons, expression of wild-type an dmutant enzymes in Escherichia coli strain XL 1-Blue
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
EXTERNAL LINKS (specific for EC-Number 3.4.21.72)
Transporter Classification Database (TCDB): 1.B.12.3.1
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Release 2023.1 (January 2023)
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