Information on EC 3.4.21.B3 - duodenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.21.B3
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
duodenase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
proteolytic cleavage of polypeptides to large and stable peptides, preferential cleavage sites: Lys-, Arg-, Tyr-, Phe-, Leu-, -Pro
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
146702-80-9
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
possible participation of duodenase in the cascade of activation of digestive enzymes
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-N-acetyl-Leu-Leu-Arg-4-nitroanilide + H2O
alpha-N-acetyl-Leu-Leu-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
-
alpha-N-acetyl-Leu-Lys-Arg-4-nitroanilide + H2O
alpha-N-acetyl-Leu-Lys + Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
-
alpha-N-benzoyl-Val-Gly-Arg-4-nitroanilide + H2O
alpha-N-benzoyl-Val-Gly-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
-
alpha-N-benzyloxycarbonyl-Ala-Ala-Ala-Arg-4-nitroanilide + H2O
alpha-N-benzyloxycarbonyl-Ala-Ala-Ala-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
-
alpha-N-benzyloxycarbonyl-Ala-Ala-Ile-Arg-Arg-4-nitroanilide + H2O
alpha-N-benzyloxycarbonyl-Ala-Ala-Ile-Arg-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
-
alpha-N-succinyl-Ala-Ala-Phe-4-nitroanilide + H2O
alpha-N-succinyl-Ala-Ala-Phe + 4-nitroaniline
show the reaction diagram
-
-
-
-
-
alpha-N-succinyl-Ala-Ala-Pro-Leu-4-nitroanilide + H2O
alpha-N-succinyl-Ala-Ala-Pro-Leu + 4-nitroaniline
show the reaction diagram
-
-
-
-
-
alpha-N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
alpha-N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
show the reaction diagram
alpha-N-succinyl-Gly-Gly-Phe-4-nitroanilide + H2O
alpha-N-succinyl-Gly-Gly-Phe + 4-nitroaniline
show the reaction diagram
-
-
-
-
-
alpha-N-succinyl-Ser-Pro-Lys-4-nitroanilide + H2O
alpha-N-succinyl-Ser-Pro-Lys + 4-nitroaniline
show the reaction diagram
-
-
-
-
-
alpha-N-succinyl-Thr-Pro-Lys-4-nitroanilide + H2O
alpha-N-succinyl-Thr-Pro-Lys + 4-nitroaniline
show the reaction diagram
-
-
-
-
-
alpha-N-succinyl-Val-Pro-Phe-4-nitroanilide + H2O
alpha-N-succinyl-Val-Pro-Phe + 4-nitroaniline
show the reaction diagram
alpha-N-t-butoxycarbonyl-Gly-Phe-Arg-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
-
alpha-N-tosyl-Gly-Pro-Lys-4-nitroanilide + H2O
alpha-N-tosyl-Gly-Pro-Lys + 4-nitroaniline
show the reaction diagram
-
-
-
-
-
angiotensin II + H2O
fragments of angiotensin II
show the reaction diagram
-
enzyme cleaves bond between residues 2-3 and 4-5
-
-
-
angiotensinogen-(1-14) + H2O
fragments of angiotensinogen-(1-14)
show the reaction diagram
bovine duodenase + H2O
fragments of bovine duodenase
show the reaction diagram
-
enzyme cleaves bond between residues 14-15, 17-18, 63-64, 70-71, 110-111, 138-139, 157-158, 162-163, 174-175 and 197-198
-
-
-
bovine proenteropeptidase + H2O
enteropeptidase fragments
show the reaction diagram
-
inactive protease substrate from bovine duodenal mucosa, recombinant 150 kDa glycoprotein
activated protease, cleaved into 2 fragments corresponding to heavy and light chain of the enteropeptidase, 130-140 kDa and 43 kDa
-
-
Bovine serum albumin + H2O
?
show the reaction diagram
-
-
-
-
?
bovine serum albumin + H2O
fragments of bovine serum albumin
show the reaction diagram
Escherichia coli La-protease + H2O
fragments of Escherichia coli La-protease
show the reaction diagram
-
enzyme cleaves bond between residues 219-220 and 239-240
-
-
-
FMRF-NH2 + H2O
?
show the reaction diagram
-
-
-
-
-
glucagon + H2O
fragments of glucagon
show the reaction diagram
human gamma-interferon + H2O
fragments of human gamma-interferon
show the reaction diagram
-
enzyme cleaves bond between residues 69-70
-
-
-
human interleukin II-(59-79) + H2O
fragments of human interleukin II-(59-79)
show the reaction diagram
-
enzyme cleaves bond between residues 66-67
-
-
-
human proinsulin + H2O
fragments of human proinsulin
show the reaction diagram
-
cleaved bonds, overview
-
-
-
LEEELKPLEEVLNL + H2O
LEEELKPL + EEVLNL
show the reaction diagram
-
-
-
-
-
LVTQEVSPKIVGGS + H2O
?
show the reaction diagram
-
-
-
-
-
melittin + H2O
fragments of melittin
show the reaction diagram
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
?
show the reaction diagram
-
-
-
-
?
N-succinyl-Thr-Pro-Lys-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
Naja naja oxiana neurotoxin II + H2O
fragments of Naja naja oxiana neurotoxin II
show the reaction diagram
-
enzyme cleaves bond between residues 15-16, 26-27, 44-45, and 32-33
-
-
-
polypeptide + H2O
peptides
show the reaction diagram
porcine proinsulin + H2O
fragments of porcine proinsulin
show the reaction diagram
protease-activated receptor-1 + H2O
?
show the reaction diagram
-
-
-
-
?
surfagon + H2O
fragments of surfagon
show the reaction diagram
-
enzyme cleaves bond between residues 3-4
-
-
-
tosyl-Gly-Pro-Arg-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
tosyl-Gly-Pro-Lys + p-nitroaniline
show the reaction diagram
-
-
-
-
?
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
polypeptide + H2O
peptides
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha-N-tosyl-L-lysine chloromethane
Alpha1-antitrypsin
-
-
-
antichymotrypsin
-
-
-
antichymotrypsin P2-P3'
-
-
-
antichymotrypsin P3-P4'
-
-
-
antichymotrypsin P4-P3'
-
-
-
antichymotrypsin P6-P4'
-
-
-
Bowman Birk soybean inhibitor
-
chymostatin
-
-
chymotrypsin inhibitor
-
form I and II from potato, from kidney bean
-
diisopropylphosphofluoridate
EDTA
-
weak inhibition at high concentration
Human alpha1-proteinase inhibitor
-
suicide mechanism, regulatory effect
-
Human alpha2-macroglobulin
-
complete inhibition in less than 30 s at equimolar ratio of the inhibitior and enzyme
-
inhibitor-chymotrypsin complex
-
no inhibition of trypsin-like and chymotrypsin-like activity by EDTA, Ca2+, and benzamidine
-
Kunitz type soybean trypsin inhibitor
-
o-phenanthroline
-
weak
phenylmethanesulfonyl fluoride
soybean Bauman-Birk protease inhibitor
-
40% reduced activity in the presence of 0.6 mM
-
Trypsin inhibitor
-
white ovomucoid
-
from chicken egg
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10.4
alpha-N-acetyl-Leu-Leu-Arg-4-nitroanilide
-
pH 8.0, 37°C
3.2
alpha-N-acetyl-Leu-Lys-Arg-4-nitroanilide
-
pH 8.0, 37°C
0.54
alpha-N-benzoyl-Val-Gly-Arg-4-nitroanilide
-
pH 8.0, 37°C
0.28 - 1.1
alpha-N-benzyloxycarbonyl-Ala-Ala-Ala-Arg-4-nitroanilide
0.8 - 1.3
alpha-N-succinyl-Ala-Ala-Phe-4-nitroanilide
1.1
alpha-N-succinyl-Ala-Ala-Pro-Leu-4-nitroanilide
-
pH 8.0, 37°C
0.56 - 1.1
alpha-N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
1.5
alpha-N-succinyl-Gly-Gly-Phe-4-nitroanilide
-
pH 8.0, 37°C
1
alpha-N-succinyl-Ser-Pro-Lys-4-nitroanilide
-
pH 8.0, 37°C
0.39
alpha-N-succinyl-Ser-Thr-Pro-Lys-4-nitroanilide
-
pH 8.0, 37°C
1.2
alpha-N-succinyl-Val-Pro-Phe-4-nitroanilide
-
pH 8.0, 37°C
0.2
alpha-N-t-butoxycarbonyl-Gly-Phe-Arg-4-nitroanilide
-
pH 8.0, 37°C
0.37
alpha-N-tosyl-Gly-Pro-Lys-4-nitroanilide
-
pH 8.0, 25°C
0.027 - 0.042
angiotensinogen-(1-14)
0.1
FMRF-NH2
-
pH 8.0, 37°C <2>
1
LEEELKPLEEVLNL
-
pH 8.0, 37°C
0.087
LVTQEVSPKIVGGS
-
pH 8.0, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6
alpha-N-acetyl-Leu-Leu-Arg-4-nitroanilide
Bos taurus
-
pH 8.0, 37°C
1.2
alpha-N-acetyl-Leu-Lys-Arg-4-nitroanilide
Bos taurus
-
pH 8.0, 37°C
6
alpha-N-benzoyl-Val-Gly-Arg-4-nitroanilide
Bos taurus
-
pH 8.0, 37°C
14.4
alpha-N-benzyloxycarbonyl-Ala-Ala-Ala-Arg-4-nitroanilide
Bos taurus
-
pH 8.0, 37°C
3.6 - 13.8
alpha-N-succinyl-Ala-Ala-Phe-4-nitroanilide
1.2
alpha-N-succinyl-Ala-Ala-Pro-Leu-4-nitroanilide
Bos taurus
-
pH 8.0, 37°C
9 - 68.4
alpha-N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
3.6
alpha-N-succinyl-Gly-Gly-Phe-4-nitroanilide
Bos taurus
-
pH 8.0, 37°C
156
alpha-N-succinyl-Ser-Pro-Lys-4-nitroanilide
Bos taurus
-
pH 8.0, 37°C
438
alpha-N-succinyl-Ser-Thr-Pro-Lys-4-nitroanilide
Bos taurus
-
pH 8.0, 37°C
33 - 168
alpha-N-succinyl-Val-Pro-Phe-4-nitroanilide
24
alpha-N-t-butoxycarbonyl-Gly-Phe-Arg-4-nitroanilide
Bos taurus
-
pH 8.0, 37°C
126 - 186
angiotensinogen-(1-14)
4.2
FMRF-NH2
Bos taurus
-
pH 8.0, 37°C
60
LEEELKPLEEVLNL
Bos taurus
-
pH 8.0, 37°C
84
LVTQEVSPKIVGGS
Bos taurus
-
pH 8.0, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000013
Alpha1-antitrypsin
-
in 0.01 M acetate buffer, pH 4.5, at 25°C
-
0.00033
antichymotrypsin P2-P3'
-
in 0.01 M acetate buffer, pH 4.5, at 25°C
-
0.0019
antichymotrypsin P3-P4'
-
in 0.01 M acetate buffer, pH 4.5, at 25°C
-
0.00043
antichymotrypsin P4-P3'
-
in 0.01 M acetate buffer, pH 4.5, at 25°C
-
0.033
antichymotrypsin P6-P4'
-
in 0.01 M acetate buffer, pH 4.5, at 25°C
-
0.0000027 - 0.000004
Bowman Birk soybean inhibitor
-
pH 8.0, 25°C
-
0.0004
Bowman Birk soybean inhibitor-trypsin complex
-
pH 8.0, 25°C
-
0.000013
Human alpha1-proteinase inhibitor
-
pH 8.0, 25°C
-
0.002
Kunitz soybean trypsin inhibitor
-
pH 8.0, 37°C
-
0.00004
Kunitz type soybean trypsin inhibitor
-
pH 8.0, 25°C
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.162
-
purified enzyme
53
-
purified enzyme, substrate Ac-Leu-Lys-Arg-4-nitroanilide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
-
broad optimum at pH 8.0-10.5, maximum at pH 10.0
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.9 - 8.2
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
epitheliocytes of Brunner's glands in human duodenal mucosa
Manually annotated by BRENDA team
-
from pulmonary artery
Manually annotated by BRENDA team
-
intestinal mucosa
Manually annotated by BRENDA team
-
spindle or stellate-shaped, located pricipally in the lamina propria and submucosa
Manually annotated by BRENDA team
additional information
-
immunohistochemic tissue detection of the enzyme, bovine duodenase-specific immunofluorescence but not that of cathepsin G, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24970
-
mass spectrometry
29000
-
gel filtration
29060
-
amino acid sequence determination, without sugar chain
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion method, protein solution: 10 mg/ml, 50 mM K/Na phosphate, pH 6.7, 1 mM NaN3, 10-14% polyethylene glycol 3350, 4°C, three-dimensional structure determination by X-ray diffraction and analysis
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 10
-
stable
658592
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
10 min, in solution at neutral pH, loss of 30% activity
70
-
stable up to
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
methanol 1% v/v stabilizes the purified enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, purified enzyme, in water stable for at least 1 year, lyophilized stable for several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
at least 90% purity
-
CM Sepharose FF column chromatography, STI Sepharose 6B column chromatography
-
to homogeneity
-
two chromatographic steps
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysi; DNA and amino acid sequence determination and analysis
DNA and amino acid sequence determination and analysis
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
comparative evaluation of specificity of different proteases can give rise to methods employing new proteases in analytical protein chemistry
biotechnology
-
comparative evaluation of specificity of different proteases can give rise to methods employing new proteases in biotechnology