Information on EC 3.4.23.19 - Aspergillopepsin II

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The expected taxonomic range for this enzyme is: Aspergillus niger

EC NUMBER
COMMENTARY hide
3.4.23.19
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RECOMMENDED NAME
GeneOntology No.
Aspergillopepsin II
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
preferential cleavage in B chain of insulin: Asn3-/-Gln, Gly13-/-Ala, Tyr26-/-Thr
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
9025-49-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
angiotensin II + H2O
DRVYIH + Pro-Phe
show the reaction diagram
-
-
-
-
?
bovine pancreatic ribonuclease A + H2O
?
show the reaction diagram
casein + H2O
hydrolyzed casein
show the reaction diagram
-
-
-
-
Hemoglobin + H2O
?
show the reaction diagram
Hemoglobin + H2O
Hydrolyzed hemoglobin
show the reaction diagram
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acid denatured hemoglobin
-
-
Milk casein + H2O
?
show the reaction diagram
-
-
-
?
oxidized in sulin B chain A + H2O
?
show the reaction diagram
-
-
-
?
oxidized insulin B chain + H2O
FVN + QHLCGSHLVE + ALYLVCGERGFFY + TPKA
show the reaction diagram
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substrate from Bos taurus, cleavage site specificity
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-
?
Oxidized insulin B-chain + H2O
Hydrolyzed insulin B-chain
show the reaction diagram
oxidized pancreatic ribonuclease A + H2O
?
show the reaction diagram
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substrate from Bos taurus
-
-
?
RGFFHTPRA + H2O
?
show the reaction diagram
-
-
-
?
RGFFTPRA + H2O
?
show the reaction diagram
-
-
-
?
RGFFYTPRA + H2O
?
show the reaction diagram
-
-
-
?
RGFMTPRA + H2O
?
show the reaction diagram
-
-
-
?
substance P + H2O
RPKPQQFF + Gly-Leu-Met
show the reaction diagram
-
-
-
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?
additional information
?
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2-epoxy-3-(4-nitrophenoxy)propane
Diazoacetyl-DL-norleucine methyl ester
DL-1-Diazo-3-tosylamido-2-heptanone
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L-1-Diazo-3-tosylamido-4-phenyl-2-butanone
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synthetic propeptides
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wild-type sequence Ala1-Asn41 and diverse truncated or mutated propeptides, overview, Ala1-Asn41 shows specific competitive inhibition, while mutants, especially R19A and H20A, show weak inhibitory effects, detailed overview
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additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.016
RGFFHTPRA
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pH 1.8, 37C
0.07
RGFFTPRA
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pH 1.8, 37C
0.33
RGFFYTPRA
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pH 1.8, 37C
0.016
RGFMTPRA
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pH 1.8, 37C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.19
RGFFHTPRA
Aspergillus niger
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pH 1.8, 37C
0.48
RGFFTPRA
Aspergillus niger
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pH 1.8, 37C
0.54 - 6.08
RGFFYTPRA
0.26
RGFMTPRA
Aspergillus niger
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pH 1.8, 37C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000027
synthetic propeptide Ala1-Asn24
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pH 4.0, 30C
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additional information
additional information
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inhibition kinetics of truncated or mutated propeptides, detailed overview
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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activities of wild-type and mutant enzymes, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.1
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substrate hemoglobin
1.8
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substrate hemoglobin
2.6
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milk casein as substrate
5.3
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hemoglobin as substrate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH profile
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
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substrate casein, pH 1.5
70
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substrate casein, pH 2.6
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55 - 65
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large decrease in activity at 60-65C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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proctase powder, crude enzyme powder from waters of Koji cultures
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22260
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amino acid sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Aspergillus niger var. macrosporus
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purified enzyme, 100 mg/ml protein in 1.4 M ammonium sulfate, 5% v/v dimethyl sulfoxide, 50 mM glycine, pH 2.1, hanging drop vapour diffusion method, X-ray diffraction structure determination and analysis at 1.4 A resolution, modeling
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
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stable up to, unstable above with rapid irreversible inactivation
668805
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native extracellular enzyme from culture medium
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native extracellular enzyme from culture medium by ammonium sulfate fractionation, sulfoethyl resin chromatography, and repeated anion exchange chromatography
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recombinant wild-type and mutant enzymes including denaturation and refolding
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNA cloning with pAR2113, Escherichia coli BL21(DE) expression system
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DNA and amino acid sequence determination and analysis, expression in Escherichia coli
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expression of wild-type and mutant enzymes
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wild-type and mutant pro-enzymes expressed in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D123A
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site-directed mutagenesis, activity is almost at background levels
D123E
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site-directed mutagenesis, activity not detectable, below 0.2%
D123E/E219D
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site-directed mutagenesis, weak activity against acid-denatured hemoglobin
D123N
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site-directed mutagenesis
D125N
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site-directed mutagenesis, markedly active toward acid-denatured hemoglobin
D137N
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site-directed mutagenesis, markedly active toward acid-denatured hemoglobin
D148N
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site-directed mutagenesis, markedly active toward acid-denatured hemoglobin
D160N
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site-directed mutagenesis, markedly active toward acid-denatured hemoglobin
D170N
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site-directed mutagenesis, markedly active toward acid-denatured hemoglobin
D208N
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site-directed mutagenesis
D220N
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site-directed mutagenesis, markedly active toward acid-denatured hemoglobin
D225N
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site-directed mutagenesis
D254N
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site-directed mutagenesis
E128Q
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site-directed mutagenesis
E141Q
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site-directed mutagenesis
E152Q
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site-directed mutagenesis, markedly active toward acid-denatured hemoglobin
E177Q
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site-directed mutagenesis
E189Q
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site-directed mutagenesis, markedly active toward acid-denatured hemoglobin
E206Q
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site-directed mutagenesis
E211Q
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site-directed mutagenesis
E2154A
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site-directed mutagenesis
E219A
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site-directed mutagenesis, activity is almost at background levels
E219D
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site-directed mutagenesis, activity not detectable, below 0.2%
E219Q
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site-directed mutagenesis
E222Q
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site-directed mutagenesis, markedly active toward acid-denatured hemoglobin
Q24E
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site-directed mutagenesis
D123N
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E219A
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site-directed mutagenesis, proform mutant, inactive mutant
E219Q
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site-directed mutagenesis, proform mutant, inactive mutant
N213A
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site-directed mutagenesis, proform mutant, the mutant shows reduced activity compared to the wild-type enzyme
N65A
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site-directed mutagenesis, proform mutant, the mutant shows increased activity compared to the wild-type enzyme
Q133A
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site-directed mutagenesis, proform mutant, inactive mutant
Q133E
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site-directed mutagenesis, proform mutant, inactive mutant
Q133E/E219Q
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site-directed mutagenesis, proform mutant, inactive mutant
S162A
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site-directed mutagenesis, proform mutant, the mutant shows reduced activity compared to the wild-type enzyme
S167A
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site-directed mutagenesis, proform mutant, the mutant shows reduced activity compared to the wild-type enzyme
T126A
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site-directed mutagenesis, proform mutant, the mutant shows reduced activity compared to the wild-type enzyme
T134A
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site-directed mutagenesis, proform mutant, the mutant shows similar activity compared to the wild-type enzyme
T192A
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site-directed mutagenesis, proform mutant, the mutant shows increased activity compared to the wild-type enzyme
T268A
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site-directed mutagenesis, proform mutant, the mutant shows reduced activity compared to the wild-type enzyme
Y151F
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site-directed mutagenesis, proform mutant, the mutant shows reduced activity compared to the wild-type enzyme
Y154F
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site-directed mutagenesis, proform mutant, the mutant shows reduced activity compared to the wild-type enzyme
Y291F
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site-directed mutagenesis, proform mutant, the mutant shows reduced activity compared to the wild-type enzyme
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes, denaturation by 8 M urea, refolding after dialysis in 50 mM sodium acetate, pH 5.3, 10 mM 2-mercaptoethanol, at 4C overnight
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