Information on EC 3.4.23.18 - Aspergillopepsin I

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The expected taxonomic range for this enzyme is: Aspergillus

EC NUMBER
COMMENTARY hide
3.4.23.18
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RECOMMENDED NAME
GeneOntology No.
Aspergillopepsin I
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydrolysis of proteins with broad specificity. Generally favours hydrophobic residues in P1 and P1', but also accepts Lys in P1, which leads to activation of trypsinogen. Does not clot milk
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY hide
9025-49-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain B
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-
Manually annotated by BRENDA team
strain 365-U-64-1
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-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Angiotensin + H2O
?
show the reaction diagram
-
cleavage site: Tyr-Ile, not His-Pro, Aspergillus oryzae enzyme, cleavage specificity compared to pepsin and cathepsin D
-
-
-
Angiotensin II + H2O
?
show the reaction diagram
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cleavage site: Tyr4-Ile5
-
-
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Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser + H2O
?
show the reaction diagram
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i.e. tetradecapeptide of a renin substrate, cleavage sites: Tyr-Ile, His-Pro, Leu-Val, Aspergillus oryzae enzyme, cleavage specificity compared to pepsin and cathepsin D
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-
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Benzyloxycarbonyl-Ala-Ala-Lys-Ala-Ala-Ala + H2O
Benzyloxycarbonyl-Ala-Ala-Lys + Ala-Ala-Ala
show the reaction diagram
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best substrate
-
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Benzyloxycarbonyl-Ala-Ala-Phe-Phe 3-(4-pyridyl)propyl ester + H2O
Benzyloxycarbonyl-Ala-Ala-Phe + Phe 3-(4-pyridyl)propyl ester
show the reaction diagram
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-
-
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Benzyloxycarbonyl-Ala-Lys-Ala-Ala-Ala + H2O
Benzyloxycarbonyl-Ala-Lys + Ala-Ala-Ala
show the reaction diagram
-
-
-
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Benzyloxycarbonyl-His-Phe-Phe ethyl ester + H2O
Benzyloxycarbonyl-His-Phe + Phe ethyl ester
show the reaction diagram
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-
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Benzyloxycarbonyl-Lys-Ala-Ala + H2O
Benzyloxycarbonyl-Lys + Ala-Ala
show the reaction diagram
Benzyloxycarbonyl-Lys-Ala-Ala-Ala + H2O
Benzyloxycarbonyl-Lys + Ala-Ala-Ala
show the reaction diagram
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-
-
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Benzyloxycarbonyl-Lys-Ala-Ala-Ala-Ala + H2O
Benzyloxycarbonyl-Lys + Ala-Ala-Ala-Ala
show the reaction diagram
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poor substrate
-
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Benzyloxycarbonyl-Lys-Leu-Ala + H2O
Benzyloxycarbonyl-Lys + Leu-Ala
show the reaction diagram
Benzyloxycarbonyl-Lys-Leu-Ala-Ala + H2O
Benzyloxycarbonyl-Lys + Leu-Ala-Ala
show the reaction diagram
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-
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Benzyloxycarbonyl-Lys-Phe-Ala + H2O
Benzyloxycarbonyl-Lys + Phe-Ala
show the reaction diagram
casein + H2O
?
show the reaction diagram
Chymotrypsinogen + H2O
Pi-Chymotrypsin
show the reaction diagram
chymotrypsinogen A + H2O
chymotrypsin + peptide fragment
show the reaction diagram
Cytochrome c + H2O
?
show the reaction diagram
Dnp-Ala-Ala-Phe-Phe-Ala-Arg-NH2 + H2O
Dnp-Ala-Ala-Phe + Phe-Ala-Arg-NH2
show the reaction diagram
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chromogenic synthetic peptide substrate
-
-
?
DRVYIHPFHLLVYS + 3 H2O
DRVY + Ile-His + PFHLL + Val-Tyr-Ser
show the reaction diagram
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tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
-
-
?
DRVYIHPFHLLVYS + 3 H2O
DRVY + Ile-His + PFHLL + VYS
show the reaction diagram
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + 3 H2O
FVNQHLCGSHLVEAL + Tyr + LVCGERGF + FYTPKA
show the reaction diagram
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substrate is the oxidized insulin B chain, primarily cleavage at Leu15-Tyr16 and Phe24-Phe25, and minor cleavage of Tyr16-Leu17, overview
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?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
FVNQHLCGSH + LVEA + Leu + Tyr + LVCGERGF + FYTPKA
show the reaction diagram
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substrate is the oxidized insulin B chain, cleavage site specificity, overview
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-
?
Hemoglobin + H2O
?
show the reaction diagram
Oxidized insulin B-chain + H2O
Hydrolyzed insulin B-chain
show the reaction diagram
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major cleavage sites: Phe24-Phe25, Leu15-Tyr16, minor sites: Ala14-Leu15, Tyr16-Leu17, peptide bond specificity compared to other proteinases
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Proangiotensin + H2O
?
show the reaction diagram
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cleavage sites: Tyr-Ile and His-Pro, Aspergillus oryzae enzyme, cleavage specificity compared to pepsin and cathepsin D
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proangiotensin + H2O
DRVYIH + PFHLLVYS
show the reaction diagram
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the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
i.e. angiotensin I
-
?
tert-Butoxycarbonyl-Ile-Glu-Gly-Arg 4-methylcoumarin 7-amide + H2O
tert-Butoxycarbonyl-Ile-Glu-Gly + Arg 4-methylcoumarin 7-amide
show the reaction diagram
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-
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tert-Butoxycarbonyl-Leu-Ser-Thr-Arg 4-methylcoumarin 7-amide + H2O
tert-Butoxycarbonyl-Leu-Ser-Thr + Arg 4-methylcoumarin 7-amide
show the reaction diagram
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-
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Trypsinogen + H2O
?
show the reaction diagram
trypsinogen + H2O
trypsin + peptide fragment
show the reaction diagram
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activation by cleavage of a Lys-Pro bond
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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
chymotrypsinogen A + H2O
chymotrypsin + peptide fragment
show the reaction diagram
DRVYIHPFHLLVYS + 3 H2O
DRVY + Ile-His + PFHLL + Val-Tyr-Ser
show the reaction diagram
-
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
-
-
?
DRVYIHPFHLLVYS + 3 H2O
DRVY + Ile-His + PFHLL + VYS
show the reaction diagram
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + 3 H2O
FVNQHLCGSHLVEAL + Tyr + LVCGERGF + FYTPKA
show the reaction diagram
-
substrate is the oxidized insulin B chain, primarily cleavage at Leu15-Tyr16 and Phe24-Phe25, and minor cleavage of Tyr16-Leu17, overview
-
-
?
proangiotensin + H2O
DRVYIH + PFHLLVYS
show the reaction diagram
-
the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
i.e. angiotensin I
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?
trypsinogen + H2O
trypsin + peptide fragment
show the reaction diagram
-
activation by cleavage of a Lys-Pro bond
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?
additional information
?
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the extracellular enzyme pays a role in development of aspergillosis in lung of mammalia, but it is not essential for virulence
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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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in the presence of Cu2+
L-1-Diazo-3-tosylamido-4-phenyl-2-butanone
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in the presence of Cu2+
N-Acetylimidazole
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N-bromosuccinimide
Pepstatin
pepstatin A
specific inhibition of the mature enzyme
Streptomyces pepsin inhibitor
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additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cholesterol
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activation, acetone-washed membrane-bound enzyme
Diglycerides
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activation, acetone-washed membrane-bound enzyme
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monoglycerides
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activation, acetone-washed membrane-bound enzyme
Phospholipids
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activation, acetone-washed membrane-bound enzyme
Triton X-100
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.5 - 4.5
Benzyloxycarbonyl-Ala-Ala-Lys-Ala-Ala-Ala
3.4 - 10.9
Benzyloxycarbonyl-Ala-Lys-Ala-Ala-Ala
8.2 - 10.6
Benzyloxycarbonyl-Lys-Ala-Ala-Ala
4.1 - 4.3
Benzyloxycarbonyl-Lys-Leu-Ala-Ala
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Aspergillus niger
0.18
chymotrypsinogen
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35°C, pH 3.5
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0.55
hemoglobin
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0.0125 - 0.1
Trypsinogen
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.32 - 30.5
Benzyloxycarbonyl-Ala-Ala-Lys-Ala-Ala-Ala
0.46 - 2.18
Benzyloxycarbonyl-Ala-Lys-Ala-Ala-Ala
0.044 - 0.17
Benzyloxycarbonyl-Lys-Ala-Ala-Ala
0.38 - 0.67
Benzyloxycarbonyl-Lys-Leu-Ala-Ala
1.14
chymotrypsinogen
Aspergillus oryzae
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35°C, pH 3.5
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11.3
Trypsinogen
Aspergillus oryzae
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35°C, pH 3.5
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
143
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enzyme form M1, in the presence of Triton X-100
867
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enzyme form M2, in the presence of Triton X-100
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.3
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hemoglobin
2.5 - 3
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substrate milk casein
2.8 - 3.4
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3
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cytochrome c
3.2 - 3.6
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chymotrypsin, 25°C
3.2
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cytochrome c
4 - 5
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synthetic peptides
4 - 4.5
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substrates trypsinogen and chymotrypsinogen
4.2
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urea-denatured hemoglobin
4.5
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urea-denatured hemoglobin
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.6 - 4
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about half-maximal activity at pH 1.6 and 4, no activity below pH 1 and above 5
2.3 - 4.3
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about half-maximal activity at pH 2.3 and 4.3, cytochrome c
3.5 - 6.5
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about half-maximal activity at pH 3.5 and 6.5, urea-denatured hemoglobin
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
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assay at
37
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
enzyme synthesis during formation of germ tubes, the pH droops during germination from pH 5.5 to pH 3.5
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
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Aspergillus oryzae, enzyme form A2, sedimentation analysis
33790
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amino acid sequence
34200
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Aspergillus saitoi, sedimentation equilibrium, meniscus depletion methods
34302
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x * 34302, amino acid sequence calculation
34500
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Aspergillus saitoi, gel filtration
35000
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Aspergillus kawachii, gel filtration, HPLC
37500
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Aspergillus fumigatus
39400
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Aspergillus oryzae, sedimentation equilibrium meniscus depletion method
41000
x * 42000, proenzyme, SDS-PAGE, x * 41000, mature enzyme, SDS-PAGE
43000
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x * 43000, SDS-PAGE
60000
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Aspergillus oryzae, enzyme form F1, gel filtration
63000
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Aspergillus oryzae, enzyme form A1, sedimetation analysis
100000
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Aspergillus oryzae, enzyme form M2, gel filtration
230000
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Aspergillus oryzae, Triton X-100 treated enzyme, gel filtration
2000000
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Aspergillus oryzae, enzyme form M1, gel filtration
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 35000, Aspergillus kawachii, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Aspergillus oryzae
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vapor diffusion method, crystallized in an orthorhombic system, space group P2(1)2(1)2(1), cell dimensions a : 49.4A, be : 79.4 A, c : 93.6 A, soaking method in complex with inhibitor pepstatin, crystals are transformed into a monoclinic system with space group C2 and cell dimensions of a : 106.8 A, be : 38.6 A, c : 78.7 A
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crystal structure determination and analysis at 2.18 A resolution
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sitting-drop vapour diffusion, trapezoid shaped crystals, unit-cell parameters a : 82.19 A, b : 36.62 A, c : 104.94 A
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.5 - 6
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fairly stable
668812
2.6 - 5
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stable in this range
30563
3 - 6
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stable in this range, complete inactivation below 2 and above 7
30575
4
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most stable at
30564
4.9
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most stable at
30562
6 - 7
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above pH 7 denaturation and inactivation
30564
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 25
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pH 2.7, 16 h stable
30
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pH 7, drastic decrease of activity probably due to autolytic activity
40
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below, stable
50
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up to, stable, at pH 3.8
60
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20 min, at pH 2.8, complete inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Casein stabilizes
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Photooxidation at pH 5.5 inactivates
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Stable to low urea concentrations, but 5 M, at an apparent pH of 5.5 inactivates 46% after 30 min and 59% after 60 min incubation
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, in 50 mM sodium acetate, pH 5, stable
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20-25°C, pH 2.7, 16 h
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cytoplasmic enzyme: partial; several isoforms (cytoplasmic F1 and F2); several isoforms (extracellular A1 and A2)
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from crude powder preparation
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from koji culture and submerged cell culture
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from Molsin, a commercial crude enzyme extract
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recombinant enzyme from Escherichia coli after solubilization from inclusion bodies by ion exchange chromatography to homogeneity
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several isoforms (extracellular A1 and A2)
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several isoforms (membrane-bound M1 and M2)
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, phylogenetic analysis of Aspergillus
gene apnS, DNA and amino acid sequence determination and analysis, phylogenetic analysis of Aspergillus, expression of the proenzyme in Saccharomyces cerevisiae, and in Escherichia coli inclusion bodies, expression of the N-terminal sequence in Escherichia coli
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gene pepA, located on chromosome 1, DNA and amino acid sequence determination and analysis, genetic organization, phylogenetic analysis of Aspergillus
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proctase B, DNA and amino acid sequence determination and analysis, phylogenetic analysis of Aspergillus
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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gene disruption leads to 85% reduced extracellular proteolytic activity
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli inclusion bodies by solubilization with 8 M urea and dialysis
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nutrition