Information on EC 3.4.24.13 - IgA-specific metalloendopeptidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.24.13
-
RECOMMENDED NAME
GeneOntology No.
IgA-specific metalloendopeptidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Cleavage of Pro-/-Thr bond in the hinge region of the heavy chain of human IgA
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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endopeptidase; peptides, endopeptidase
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CAS REGISTRY NUMBER
COMMENTARY hide
72231-73-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain CCUG4815
UniProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
strain NMB
-
-
Manually annotated by BRENDA team
no activity in Moraxella catarrhalis
basonym: Branhamella catarrhalis
-
-
Manually annotated by BRENDA team
no activity in Streptococcus australis
-
-
-
Manually annotated by BRENDA team
no activity in Streptococcus cristatus
-
-
-
Manually annotated by BRENDA team
no activity in Streptococcus gordonii
-
-
-
Manually annotated by BRENDA team
no activity in Streptococcus oligofermentans
-
-
-
Manually annotated by BRENDA team
no activity in Streptococcus parasanguinis
-
-
-
Manually annotated by BRENDA team
no activity in Streptococcus peroris
-
-
-
Manually annotated by BRENDA team
no activity in Streptococcus suis
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Streptococcus mitior
-
-
-
Manually annotated by BRENDA team
strain SK564; strain SK564
SwissProt
Manually annotated by BRENDA team
strain SK609; strain SK609
SwissProt
Manually annotated by BRENDA team
strain SK1
-
-
Manually annotated by BRENDA team
serotype 2 , strain 05ZYS
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-
Manually annotated by BRENDA team
serotype 2 , strain 05ZYS
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Dabcyl-gammaPRPPAPVFY-Edans + H2O
Dabcyl-gammaPRPP + APVFY-Edans
show the reaction diagram
human IgA1 + H2O
?
show the reaction diagram
human IgA1 with CH3 domain exchanged for that of human IgG1 + H2O
?
show the reaction diagram
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
show the reaction diagram
human monoclonal capsule-specific IgA + H2O
?
show the reaction diagram
-
-
-
-
?
IgA2-IgA1 half hinge + H2O
?
show the reaction diagram
Immunoglobulin A1 + H2O
?
show the reaction diagram
immunoglobulin A1 + H2O
immunoglobulin A1 Fabalpha fragments + immunglobulin A1 Fcalpha
show the reaction diagram
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
show the reaction diagram
immunoglobulin IgA1 + H2O
effector domain of IgA1 + Fab determinants of IgA1
show the reaction diagram
-
-
specific cleavage of hinge region. IgA1 bound to bacterial porin A is masked by the serogroup B polysaccharide capsule and less accessible to degradation. De novo synthesis of enzyme is required for degradation of porin-A-bound IgA1, specific cleavage of hinge region
-
?
IQADVPSVPSNNEEIY + H2O
IQADVP + SVPSNNEEIY
show the reaction diagram
LAMP1 + H2O
?
show the reaction diagram
LPRPPAPVFSY + H2O
LPRP + PAPVFSY
show the reaction diagram
NIVVAPPSPQANQAEEY + H2O
NIVVAPP + SPQANQAEEY
show the reaction diagram
polymeric IgA + H2O
?
show the reaction diagram
PPAPVY + H2O
Pro-Pro + APVY
show the reaction diagram
-
-
-
?
PRPPAPVFSLDY + H2O
PRP + PAPVFSLDY
show the reaction diagram
-
-
-
?
RAILPRPPAPVFSLDDY + H2O
RAILPRPP + APVFSLDDY
show the reaction diagram
-
-
-
?
RAILPRPPAPVFY + H2O
RAILPRPP + APVFY
show the reaction diagram
-
-
-
?
secretory IgA + H2O
?
show the reaction diagram
additional information
?
-
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
-
IgA1 protease is a proteolytic enzyme with strict substrate specificity for human IgA1
-
-
?
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
show the reaction diagram
Immunoglobulin A1 + H2O
?
show the reaction diagram
immunoglobulin A1 + H2O
immunoglobulin A1 Fabalpha fragments + immunglobulin A1 Fcalpha
show the reaction diagram
-
-
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
show the reaction diagram
immunoglobulin IgA1 + H2O
effector domain of IgA1 + Fab determinants of IgA1
show the reaction diagram
-
-
specific cleavage of hinge region. IgA1 bound to bacterial porin A is masked by the serogroup B polysaccharide capsule and less accessible to degradation. De novo synthesis of enzyme is required for degradation of porin-A-bound IgA1
-
?
LAMP1 + H2O
?
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
1,2-diethyl-3-hydroxypyridine-4(1H)-thione
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1-ethyl-3-hydroxy-2-methylpyridine-4(1H)-thione
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1-[2-(3-bromophenyl)ethyl]-3-hydroxy-2-methylpyridine-4(1H)-thione
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1-[2-(3-chloro-4-methoxyphenyl)ethyl]-3-hydroxy-2-methylpyridine-4(1H)-thione
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1-[2-(3-chlorophenyl)ethyl]-3-hydroxy-2-methylpyridine-4(1H)-thione
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1-[2-(3-fluorophenyl)ethyl]-3-hydroxy-2-methylpyridine-4(1H)-thione
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2,2'-dipyridyldisulfide
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3,4-dichloroisocoumarin
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3-hydroxy-1,2-dimethylpyridine-4(1H)-thione
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3-hydroxy-1-[2-(3-methoxyphenyl)ethyl]-2-methylpyridine-4(1H)-thione
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3-hydroxy-1-[2-(4-methoxyphenyl)ethyl]-2-methylpyridine-4(1H)-thione
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3-hydroxy-2-methyl-1-(2-phenylethyl)pyridine-4(1H)-thione
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3-hydroxy-2-methyl-1-[2-(3-methylphenyl)ethyl]pyridine-4(1H)-thione
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6-deoxy-6-demethyl-4-dimethylaminotetracycline
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i.e. CMT-3, 50% inhibition at 0.01 to 0.05 mM. Presence of 1.5 mM CaCl2 enhances inhibition
bathocuproine disulfonic acid
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diisopropylfluorophosphate
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doxycycline
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50% inhibition at 0.015 mM
Human serum
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iodoacetamide
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octyl glucoside
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p-chloromercuribenzenesulfonic acid
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peptide boronic acids
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phenylmethylsulfonyl fluoride
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0034
IgA1
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.962
1,2-diethyl-3-hydroxypyridine-4(1H)-thione
Streptococcus pneumoniae
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in 50 mM Tris-HCl, pH 7.0, at 37°C
0.887
1-ethyl-3-hydroxy-2-methylpyridine-4(1H)-thione
Streptococcus pneumoniae
-
in 50 mM Tris-HCl, pH 7.0, at 37°C
0.00614
1-[2-(3-bromophenyl)ethyl]-3-hydroxy-2-methylpyridine-4(1H)-thione
Streptococcus pneumoniae
-
in 50 mM Tris-HCl, pH 7.0, at 37°C
0.00498
1-[2-(3-chloro-4-methoxyphenyl)ethyl]-3-hydroxy-2-methylpyridine-4(1H)-thione
Streptococcus pneumoniae
-
in 50 mM Tris-HCl, pH 7.0, at 37°C
0.0043
1-[2-(3-chlorophenyl)ethyl]-3-hydroxy-2-methylpyridine-4(1H)-thione
Streptococcus pneumoniae
-
in 50 mM Tris-HCl, pH 7.0, at 37°C
0.00774
1-[2-(3-fluorophenyl)ethyl]-3-hydroxy-2-methylpyridine-4(1H)-thione
Streptococcus pneumoniae
-
in 50 mM Tris-HCl, pH 7.0, at 37°C
1.3
3-hydroxy-1,2-dimethylpyridine-4(1H)-thione
Streptococcus pneumoniae
-
in 50 mM Tris-HCl, pH 7.0, at 37°C
0.00664
3-hydroxy-1-[2-(3-methoxyphenyl)ethyl]-2-methylpyridine-4(1H)-thione
Streptococcus pneumoniae
-
in 50 mM Tris-HCl, pH 7.0, at 37°C
0.007
3-hydroxy-1-[2-(4-methoxyphenyl)ethyl]-2-methylpyridine-4(1H)-thione
Streptococcus pneumoniae
-
in 50 mM Tris-HCl, pH 7.0, at 37°C
0.0127
3-hydroxy-2-methyl-1-(2-phenylethyl)pyridine-4(1H)-thione
Streptococcus pneumoniae
-
in 50 mM Tris-HCl, pH 7.0, at 37°C
0.00914
3-hydroxy-2-methyl-1-[2-(3-methylphenyl)ethyl]pyridine-4(1H)-thione
Streptococcus pneumoniae
-
in 50 mM Tris-HCl, pH 7.0, at 37°C
0.0523
Berberine
Streptococcus pneumoniae
-
in 50 mM Tris-HCl, pH 7.0, at 37°C
0.152
norharmane
Streptococcus pneumoniae
-
in 50 mM Tris-HCl, pH 7.0, at 37°C
0.0231
remerine
Streptococcus pneumoniae
-
in 50 mM Tris-HCl, pH 7.0, at 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 7.5
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active over the range pH 4.5-7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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reverse transcriptase PCR shows that igB is transcribed in Haemophilus influenza
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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associated via an N-terminal membrane anchor, release upon proteolytic cleavage
Manually annotated by BRENDA team
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associated to external side of bacterial membrane. Localization requires the LPNTG sorting motif near the amino terminus of protein
Manually annotated by BRENDA team
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recombinant enzyme produced in Escherichia coli is localized in the periplasmic space, a sequence linked to the carboxyl terminus of the iga gene but not present in the original clone is shown to be necessary to achieve normal secretion
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
62000
-
gel filtration
70000
-
x * 70000, SDS-PAGE under reducing conditions
86000
-
gel filtration
90000
-
x * 90000, SDS-PAGE
108000
-
x * 108000, product of gene fragment missing about 1300 bp in the 3’ region, SDS-PAGE
112000
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x * 112000, type 1 protease, SDS-PAGE
114000
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x * 114000, the 114000 Da peptide is converted to a still active 109000 Da peptide during isolation, type 2 protease, SDS-PAGE
137000
-
x * 137000, SDS-PAGE
154000
-
predicted from amino acid sequence
additional information
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 62000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
4°C, stable for several days
37019
10
-
4°C, stable for several days
37019
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
about 30% loss of activity after 2 h, about 50% loss of activity after 3 h
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
recombinant proteins are highly instable
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 50 mM Tris-acetate, pH 7.5, 20% glycerol, 0.1 mM dithiothreitol, 5 mM EDTA, type 1 protease, less than 10% loss of activity after 2 weeks
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4°C, long term storage of the 109000 Da type 2 protease, breakdown yields fragments of 95000 and 15000 Da and loss of activity
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50 mM, Tris-HCl, pH 7.5, 20% glycerol, stable for at least 2 months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
-
partial; type 2 enzyme
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recombinant glutathione S-transferase fusion proteins of three segments of enzyme, comprising amino acids 1032-1964, 708-1964, and 104-1964. Segment 1032-1964 is catalytically inactive. Recombinant proteins are highly instable.
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type 1 enzyme; type 2 enzyme
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using Ni-NTA agorose binding
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as a His-tagged Haemophilus influenzae type 1 IgA1 protease
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expressed in Escherichia coli
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expressed in Escherichia coli as a His-tagged fusion protein
expressed in Escherichia coli as a His-tagged fusion protein; expressed in Escherichia coli as a His-tagged fusion protein
expressed in Escherichia coli BL21 cells
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expression in Escherichia coli
expression in Escherichia coli K-12
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expression in Escherichia coli, construction of mutants of Neisseria gonorrhoeae that fail to produce the activity
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expression in Haemophilis influenzae with His-tag. Protein is autoprocessed and secreted
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fragment missing about 1300 bp in the 3’ region, purified protein fragment is active
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the Streptococcus pneumoniae gene is 64% identical and 76% similar to that of Streptococcus sanguis. The zinc-binding sequence is conserved in the two proteins
three segments of enzyme, comprising amino acids 1032-1964, 708-1964, and 104-1964
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTA1003-1006
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mutant lacking the confirmed self-cleavage recognition site shows only little reduction in secreted protease
DELTA1005-1006
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mutant containing modified consensus recognition sites shows only slight reduction in protease secretion
DELTA974-1002
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mutant lacking the putative self-cleavage recognition site and the intervening residues shows only little reduction in secreted protease
DELTA974-978
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mutant lacking the putative self-cleavage recognition site shows only little reduction in secreted protease
DELTA974-978/DELTA1003-1007
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double deletion mutant lacking both self-cleavage recognition sites shows only a 40% reduced secretion
P1004T/S1005E/S1006A
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mutant containing modified consensus recognition sites shows only slight reduction in protease secretion
P975E/P1004E
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mutant containing modified consensus recognition sites shows 30% lower secreted protease levels than wild-type
S1005E
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mutant containing modified consensus recognition sites shows only slight reduction in protease secretion
S267V
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this mutant fails to undergo self-cleavage and shows no enzymatic activity
DELTA1005-1006
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mutant containing modified consensus recognition sites shows only slight reduction in protease secretion
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P1004T/S1005E/S1006A
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mutant containing modified consensus recognition sites shows only slight reduction in protease secretion
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S1005E
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mutant containing modified consensus recognition sites shows only slight reduction in protease secretion
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S267V
-
this mutant fails to undergo self-cleavage and shows no enzymatic activity
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E1605A
-
of segment 708-1964, completely inactive
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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