Information on EC 3.4.21.72 - IgA-specific serine endopeptidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.21.72
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RECOMMENDED NAME
GeneOntology No.
IgA-specific serine endopeptidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Cleavage of immunoglobulin A molecules at certain Pro-/- bonds in the hinge region. No small molecule substrates are known
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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-
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CAS REGISTRY NUMBER
COMMENTARY hide
55127-02-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
type XXIV
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-
Manually annotated by BRENDA team
isoform IgaA2
UniProt
Manually annotated by BRENDA team
isoform IgaA1
UniProt
Manually annotated by BRENDA team
strain MS11-N139
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-
Manually annotated by BRENDA team
no activity in Haemophilus haemolyticus
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-
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Manually annotated by BRENDA team
no activity in Neisseria gonorrhoeae
strain MS11
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-
Manually annotated by BRENDA team
no activity in Neisseria gonorrhoeae MS11
strain MS11
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-
Manually annotated by BRENDA team
no activity in Streptococcus australis
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-
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Manually annotated by BRENDA team
no activity in Streptococcus cristatus
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-
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Manually annotated by BRENDA team
no activity in Streptococcus oligofermentans
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-
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Manually annotated by BRENDA team
no activity in Streptococcus parasanguinis
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-
-
Manually annotated by BRENDA team
no activity in Streptococcus peroris
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-
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Manually annotated by BRENDA team
no activity in Streptococcus suis
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-
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Manually annotated by BRENDA team
SK10
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Manually annotated by BRENDA team
serotype 2, isolated from pig brain, gene iga
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-
Manually annotated by BRENDA team
type XIV
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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Haemophilus influenzae has likely acquired igaB from Neisseria meningitidis, the acquisition is accompanied by a about 20 kb genomic inversion that is present only in strains that have igaB, overview
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
human IgA1 + H2O
?
show the reaction diagram
human immunoglobulin A1 + H2O
?
show the reaction diagram
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
show the reaction diagram
human lamp-1 + H2O
?
show the reaction diagram
IgA1 + H2O
?
show the reaction diagram
IgA2-IgA1 half hinge + H2O
?
show the reaction diagram
immunoglobulin A + H2O
?
show the reaction diagram
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
show the reaction diagram
Immunoglobulin A1 + H2O
?
show the reaction diagram
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
show the reaction diagram
IgA proteases only cleave the proline, serine and threonine rich hinge peptide unique to immunoglobulin A1
-
-
?
mutant hhP227S + H2O
?
show the reaction diagram
mutant hhS224/230P + H2O
?
show the reaction diagram
mutant hhS224P + H2O
?
show the reaction diagram
mutant hhS230P + H2O
?
show the reaction diagram
porcine IgA1 + H2O
?
show the reaction diagram
surface-exposed SD domain + H2O
?
show the reaction diagram
the enzyme cleaves its own isolated recombinant SD domain, single or linked with the alpha-protein, giving the L1 domain
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-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
human IgA1 + H2O
?
show the reaction diagram
human immunoglobulin A1 + H2O
?
show the reaction diagram
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
show the reaction diagram
IgA1 + H2O
?
show the reaction diagram
immunoglobulin A + H2O
?
show the reaction diagram
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
show the reaction diagram
Immunoglobulin A1 + H2O
?
show the reaction diagram
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
show the reaction diagram
P44969
IgA proteases only cleave the proline, serine and threonine rich hinge peptide unique to immunoglobulin A1
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-
?
porcine IgA1 + H2O
?
show the reaction diagram
additional information
?
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,1'-Hexamethylenebis(5-[4-chlorophenyl]biguanide)
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3,4-dichloroisocoumarin
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Bathocuproine disulfonate
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Cetyltrimethylammonium bromide
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Chlorhexidine
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diisopropyl fluorophosphate
Normal human serum
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Peptide prolyl boronic acids
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Protamine sulfate
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-
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Traditional protease inhibitors
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-
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additional information
no inhibition by natural protease inhibitors SLPI, alpha-1-antitrypsin, cathepsin G and cystatin C, and by synthetic protease inhibitors Tos-Lys-chloromethylketone, and ZD0892
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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active only under reducing conditions
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0008 - 0.056
IgA
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
pI: 5.0
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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the alpha-protein domain has a pI-value of higher than 10
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
inactive pro-enzyme, the cleaved and maturated protein is secreted
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
62000
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Bacteroides melaninogenicus
80000
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and 105000, Haemophilus influenzae, HPLC gel filtration
105000
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and 80000, Haemophilus influenzae, gel filtration
106000
108700
calculated from amino acid sequence
109000
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x * 109000, calculated
120000
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x * 120000, SDS-PAGE
170000
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x * 170000, full-length protein, SDS-PAGE
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.1 M sodium acetate, pH 5.0, 0.1 M potassium dihydrogen phosphate and 10% (w/v) PEG 20000
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
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complete loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, slow loss of activity
Frozen enzyme is stable for at least 1 year
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
development and evaluation of a method for isolation and purification of IgA1 protease from a culture of Neisseria meningitidis serogroup A, purification involves absorption, hydrophobic interaction, anion exchange, and jacalin affinity chromatography steps, to homogeneity, overview
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native enzyme from three inactivated intermediates of meningococcal vaccine production
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Ni-NTA agarose column chromatography
recombinant His-tagged IgA1 protease by nickel affinity chromatography, anion exchange chromatography, and gel filtration
recombinant isolated surface-exposed SD domain from Escherichia coli to homogeneity
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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expressed in Escherichia coli Rosetta2(DE3)pLysS cells
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expression in Escherichia coli
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expression of His-tagged IgA1 protease in Escherichia coli strain C41(DE3), method development and optimization by evaluation of expression of recombinant Haemophilus influenzae IgA1 protease by combining various expression plasmids, IgA1 protease constructs, and Escherichia coli strains under multiple conditions, overview
expression of the isolated surface-exposed SD domain in Escherichia coli
expression with His-tag
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gene iga, DNA and amino acid sequence determination and analysis
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
gene igaB, DNA and amino acid sequence determination and analysis, genetic organization of the igaB locus, overview
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Haemophilus influenzae gene cloned in Escherichia coli
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Haemophilus influenzae gene; Neisseria gonorrhoeae gene in Escherichia coli
igaB, COPD strains, DNA sequence determination and analysis, sequence comparisons and relation to strain 11P6H, clonal relationship among the strains, overview
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
E1605A
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inactive
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
drug development
medicine
pharmacology
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systemically administered IgA protease is able to reduce the quantity of glomerular IgA immune complexes, both the antigen and antibody components, in a passive mouse model of IgA nephropathy
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