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Enzyme Nomenclature
Information on EC 3.4.23.18 - Aspergillopepsin I
for references in articles please use BRENDA:EC3.4.23.18
Word Map on EC 3.4.23.18
- 3.4.23.18
-
cathepsins
-
proteinases
- pepstatin
- lysosomal
-
pepsinogen
- candida
- hemoglobin
-
zymogen
- albicans
- chymosin
- rhizopus
-
aspartyl
- mucor
- endothiapepsin
- leupeptin
- angiotensinogen
-
pregnancy-associated
- penicillopepsin
-
flap
- chinensis
-
milk-clotting
-
scissile
-
procathepsin
- pusillus
- napsins
- cardunculus
- rhizomucor
- boophilus
- parasitica
- rennin
- beta-secretase
-
bilobal
-
1,2-epoxy-3-p-nitrophenoxypropane
- dan
- gastricsin
-
prosegment
- cynara
- chymostatin
- nutrition
-
plasmepsins
- microplus
-
scytalidium
- b-chain
- miehei
-
d-like
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Specify your search results
The expected taxonomic range for this enzyme is: Aspergillus
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EC NUMBER 
COMMENTARY 
3.4.23.18
-
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RECOMMENDED NAME
GeneOntology No.
Aspergillopepsin I
-
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REACTION
REACTION DIAGRAM
COMMENTARY
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
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
-
-
-
-
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
catalytic residues are Asp32 and Asp214 connected by a complex network of hydrogen bonds, a third catalytic residue is Asp76, which is essential for trypsinogen activation at pH 3.0-4.5, the active site flap plays an important role in recognition of basic P1 residues
-
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
catalytic residues are Asp32 and Asp214 connected by a complex network of hydrogen bonds, a third catalytic residue is Asp76, which is essential for trypsinogen activation at pH 3.0-4.5, the active site flap plays an important role in recognition of basic P1 residues
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
9025-49-4
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Angiotensin + H2O
?
-
cleavage site: Tyr-Ile, not His-Pro, Aspergillus oryzae enzyme, cleavage specificity compared to pepsin and cathepsin D
-
-
-
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser + H2O
?
-
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
-
-
-
Benzyloxycarbonyl-Ala-Ala-Lys-Ala-Ala-Ala + H2O
Benzyloxycarbonyl-Ala-Ala-Lys + Ala-Ala-Ala
-
best substrate
-
-
Benzyloxycarbonyl-Ala-Ala-Phe-Phe 3-(4-pyridyl)propyl ester + H2O
Benzyloxycarbonyl-Ala-Ala-Phe + Phe 3-(4-pyridyl)propyl ester
-
-
-
-
Benzyloxycarbonyl-Ala-Lys-Ala-Ala-Ala + H2O
Benzyloxycarbonyl-Ala-Lys + Ala-Ala-Ala
-
-
-
-
Benzyloxycarbonyl-His-Phe-Phe ethyl ester + H2O
Benzyloxycarbonyl-His-Phe + Phe ethyl ester
-
-
-
-
Benzyloxycarbonyl-Lys-Ala-Ala-Ala + H2O
Benzyloxycarbonyl-Lys + Ala-Ala-Ala
-
-
-
-
Benzyloxycarbonyl-Lys-Ala-Ala-Ala-Ala + H2O
Benzyloxycarbonyl-Lys + Ala-Ala-Ala-Ala
-
poor substrate
-
-
Benzyloxycarbonyl-Lys-Leu-Ala-Ala + H2O
Benzyloxycarbonyl-Lys + Leu-Ala-Ala
-
-
-
-
Dnp-Ala-Ala-Phe-Phe-Ala-Arg-NH2 + H2O
Dnp-Ala-Ala-Phe + Phe-Ala-Arg-NH2
-
chromogenic synthetic peptide substrate
-
-
?
DRVYIHPFHLLVYS + 3 H2O
DRVY + Ile-His + PFHLL + Val-Tyr-Ser
-
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
-
-
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + 3 H2O
FVNQHLCGSHLVEAL + Tyr + LVCGERGF + FYTPKA
-
substrate is the oxidized insulin B chain, primarily cleavage at Leu15-Tyr16 and Phe24-Phe25, and minor cleavage of Tyr16-Leu17, overview
-
-
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
FVNQHLCGSH + LVEA + Leu + Tyr + LVCGERGF + FYTPKA
-
substrate is the oxidized insulin B chain, cleavage site specificity, overview
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed insulin B-chain
-
major cleavage sites: Phe24-Phe25, Leu15-Tyr16, minor sites: Ala14-Leu15, Tyr16-Leu17, peptide bond specificity compared to other proteinases
-
-
Proangiotensin + H2O
?
-
cleavage sites: Tyr-Ile and His-Pro, Aspergillus oryzae enzyme, cleavage specificity compared to pepsin and cathepsin D
-
-
-
proangiotensin + H2O
DRVYIH + PFHLLVYS
-
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
-
-
-
-
tert-Butoxycarbonyl-Leu-Ser-Thr-Arg 4-methylcoumarin 7-amide + H2O
tert-Butoxycarbonyl-Leu-Ser-Thr + Arg 4-methylcoumarin 7-amide
-
-
-
-
trypsinogen + H2O
trypsin + peptide fragment
-
activation by cleavage of a Lys-Pro bond
-
-
?
Benzyloxycarbonyl-Lys-Ala-Ala + H2O
Benzyloxycarbonyl-Lys + Ala-Ala
-
poor substrate
-
-
Benzyloxycarbonyl-Lys-Ala-Ala + H2O
Benzyloxycarbonyl-Lys + Ala-Ala
-
poor substrate
-
-
Benzyloxycarbonyl-Lys-Leu-Ala + H2O
Benzyloxycarbonyl-Lys + Leu-Ala
-
-
-
-
Benzyloxycarbonyl-Lys-Leu-Ala + H2O
Benzyloxycarbonyl-Lys + Leu-Ala
-
-
-
-
Benzyloxycarbonyl-Lys-Leu-Ala + H2O
Benzyloxycarbonyl-Lys + Leu-Ala
-
-
-
-
Benzyloxycarbonyl-Lys-Phe-Ala + H2O
Benzyloxycarbonyl-Lys + Phe-Ala
-
-
-
-
Benzyloxycarbonyl-Lys-Phe-Ala + H2O
Benzyloxycarbonyl-Lys + Phe-Ala
-
-
-
-
Benzyloxycarbonyl-Lys-Phe-Ala + H2O
Benzyloxycarbonyl-Lys + Phe-Ala
-
-
-
-
Chymotrypsinogen + H2O
Pi-Chymotrypsin
-
cleavage site: Arg15-Ile16
-
-
chymotrypsinogen A + H2O
chymotrypsin + peptide fragment
-
activation
-
-
?
chymotrypsinogen A + H2O
chymotrypsin + peptide fragment
-
activation
-
-
?
DRVYIHPFHLLVYS + 3 H2O
DRVY + Ile-His + PFHLL + VYS
-
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
-
-
?
DRVYIHPFHLLVYS + 3 H2O
DRVY + Ile-His + PFHLL + VYS
-
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
-
-
?
DRVYIHPFHLLVYS + 3 H2O
DRVY + Ile-His + PFHLL + VYS
-
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
-
-
?
DRVYIHPFHLLVYS + 3 H2O
DRVY + Ile-His + PFHLL + VYS
-
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
-
-
?
Trypsinogen + H2O
?
-
cleaves Lys-Ile and liberates hexapeptide
-
-
-
additional information
?
-
-
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
-
-
-
additional information
?
-
-
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
-
-
-
additional information
?
-
-
the extracellular enzyme pays a role in development of aspergillosis in lung of mammalia, but it is not essential for virulence
-
-
-
additional information
?
-
-
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys, at pH 5.5 the enzyme shows also an elastolytic activity with elastin Congo red
-
-
-
additional information
?
-
-
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
-
-
-
additional information
?
-
-
no hydrolysis of benzyloxycarbonyl-Lys-Gly-Ala, benzyloxycarbonyl-Lys-(D)-Leu-Ala
-
-
-
additional information
?
-
-
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
-
-
-
additional information
?
-
-
the immediate turbidity levels obtained after treatments of the black currant juice samples with the Denapsin 2P preparation are in the low end of the range
-
-
-
additional information
?
-
-
no hydrolysis of benzyloxycarbonyl-Lys-Gly-Ala, benzyloxycarbonyl-Lys-(D)-Leu-Ala
-
-
-
additional information
?
-
-
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
-
-
-
additional information
?
-
-
does not require a hydrophobic amino acid in P1, P2 or P3 position, prefers substrates with hydrophobic amino acid in P1', less so in P2'
-
-
-
additional information
?
-
-
no hydrolysis of benzyloxycarbonyl-Lys-Gly-Ala, benzyloxycarbonyl-Lys-(D)-Leu-Ala
-
-
-
additional information
?
-
-
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
-
-
-
additional information
?
-
-
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys, no activity with Z-Glu-Tyr or Z-Tyr-Leu, no milk clotting
-
-
-
additional information
?
-
-
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
-
-
-
additional information
?
-
-
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys, no activity with Z-Glu-Tyr or Z-Tyr-Leu, no milk clotting
-
-
-
additional information
?
-
-
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
DRVYIHPFHLLVYS + 3 H2O
DRVY + Ile-His + PFHLL + Val-Tyr-Ser
-
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
-
-
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + 3 H2O
FVNQHLCGSHLVEAL + Tyr + LVCGERGF + FYTPKA
-
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
-
the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
i.e. angiotensin I
-
?
trypsinogen + H2O
trypsin + peptide fragment
-
activation by cleavage of a Lys-Pro bond
-
-
?
additional information
?
-
-
the extracellular enzyme pays a role in development of aspergillosis in lung of mammalia, but it is not essential for virulence
-
-
-
chymotrypsinogen A + H2O
chymotrypsin + peptide fragment
-
activation
-
-
?
chymotrypsinogen A + H2O
chymotrypsin + peptide fragment
-
activation
-
-
?
DRVYIHPFHLLVYS + 3 H2O
DRVY + Ile-His + PFHLL + VYS
-
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
-
-
?
DRVYIHPFHLLVYS + 3 H2O
DRVY + Ile-His + PFHLL + VYS
-
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
no activation by HgCl2, NaF, FeCl3, FeCl2, CoCl2, MgCl2, CaCl2, ZnSO4
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,2-epoxy-3-(4-nitrophenoxy)propane
-
the reaction is markedly inhibited by pepstatin
Diazoacetyl-DL-norleucine methyl ester
-
in the presence of Cu2+; pH-profile
Diazoacetyl-DL-norleucine methyl ester
-
in the presence of Cu2+; pH-profile; the reaction is markedly inhibited by pepstatin
Diazoacetyl-DL-norleucine methyl ester
-
in the presence of Cu2+; pH-profile
additional information
-
diisopropyl phosphofluoridate; EDTA; no inhibition by p-chloromercuribenzene sulfonate, AgNO3, 2-mercaptoethanol, PMSF
-
additional information
-
diisopropyl phosphofluoridate; EDTA; HgCl2, NaF, FeCl3, FeCl2, CoCl2, MgCl2, CaCl2, ZnSO4; monoiodoacetate, 1,10-phenanthroline, 6-aminohexanoate; PCMB
-
additional information
-
diisopropyl phosphofluoridate; monoiodoacetate, 1,10-phenanthroline, 6-aminohexanoate; PCMB
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no activation of membrane-bound enzyme by triglycerides or 1,3-dipalmitin
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.7
3.5
additional information
additional information
-
pI: 3.15 and 3.5 (isozyme A1); pI: 3.9 (isozyme A2)
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.6 - 4
-
about half-maximal activity at pH 1.6 and 4, no activity below pH 1 and above 5
3.5 - 6.5
-
about half-maximal activity at pH 3.5 and 6.5, urea-denatured hemoglobin
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
40
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
Taka-diastase, crude Aspergillus oryzae powder preparation
-
extracellular enzyme; Taka-diastase, crude Aspergillus oryzae powder preparation
-
extracellular enzyme; Taka-diastase, crude Aspergillus oryzae powder preparation
-
enzyme synthesis during formation of germ tubes, the pH droops during germination from pH 5.5 to pH 3.5
-
enzyme synthesis during formation of germ tubes, the pH droops during germination from pH 5.5 to pH 3.5
-
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
2 forms: extracellular and cytoplasmic, the cytoplasmic isozymes are immunologically related to extracellular isozyme A2
-
2 forms: extracellular and cytoplasmic, the cytoplasmic isozymes are immunologically related to extracellular isozyme A2
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Aspergillus oryzae;
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
34200
-
Aspergillus saitoi, sedimentation equilibrium, meniscus depletion methods
39400
-
Aspergillus oryzae, sedimentation equilibrium meniscus depletion method
41000
x * 42000, proenzyme, SDS-PAGE, x * 41000, mature enzyme, SDS-PAGE
42000
additional information
42000
x * 42000, proenzyme, SDS-PAGE, x * 41000, mature enzyme, SDS-PAGE
additional information
-
amino acid sequence of Aspergillus niger deduced from nucleic acid sequence compared to that of the enzymes from Aspergillus saitoi, Aspergillus oryzae and Aspergillus awamori
additional information
-
amino acid sequence of Aspergillus niger deduced from nucleic acid sequence compared to that of the enzymes from Aspergillus saitoi, Aspergillus oryzae and Aspergillus awamori
additional information
-
amino acid sequence of Aspergillus niger deduced from nucleic acid sequence compared to that of the enzymes from Aspergillus saitoi, Aspergillus oryzae and Aspergillus awamori
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
x * 42000, proenzyme, SDS-PAGE, x * 41000, mature enzyme, SDS-PAGE
additional information
peptide mass fingerprinting, and amino acid sequence determination and analysis
additional information
-
peptide mass fingerprinting, and amino acid sequence determination and analysis
-
additional information
-
secondary and three-dimensional structure determination and comparison; secondary structure analysis, three-dimensional structure comparison
additional information
-
secondary and three-dimensional structure determination and comparison; secondary structure analysis, three-dimensional structure comparison
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
glycoprotein
-
carbohydrate content: less than 0.3% (enzyme form A2), about 50% (enzyme form A1)
proteolytic modification
the secreted enzyme has a pro-sequence, and is processed pH-dependently at below pH 4.6 to the mature enzyme
proteolytic modification
-
the secreted enzyme has a pro-sequence, and is processed pH-dependently at below pH 4.6 to the mature enzyme
-
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
-
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
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
pH 7, drastic decrease of activity probably due to autolytic activity
55
55
-
10 min, in 50 mM sodium acetate buffer, pH 5; isozyme A1 loses 10% of its original activity in contrast to almost complete loss of activity of isozyme A2
55
-
10 min, in 50 mM sodium acetate buffer, pH 5; isozyme F1 retains 70%, F2 85% of original activity
55
-
10 min, in 50 mM sodium acetate buffer, pH 5; isozyme M1 retains more than 95% of its original activity, M2 is completely inactivated
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cytoplasmic enzyme: partial; several isoforms (cytoplasmic F1 and F2); several isoforms (extracellular A1 and A2)
-
recombinant enzyme from Escherichia coli after solubilization from inclusion bodies by ion exchange chromatography to homogeneity
-
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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
-
gene pepA, located on chromosome 1, DNA and amino acid sequence determination and analysis, genetic organization, phylogenetic analysis of Aspergillus
-
proctase B, DNA and amino acid sequence determination and analysis, phylogenetic analysis of Aspergillus
-
DNA and amino acid sequence determination and analysis, phylogenetic analysis of Aspergillus
-
DNA and amino acid sequence determination and analysis, phylogenetic analysis of Aspergillus
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
gene disruption leads to 85% reduced extracellular proteolytic activity
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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
LITERATURE
nutrition
nutrition
-
Aspergillus awamori and the extracellular protease play important roles in japanese food production, overview
nutrition
-
Aspergillus species and the extracellular protease play important roles in japanese food production, overview
nutrition
-
Aspergillus oryzae and the extracellular protease play important roles in japanese food production, overview
nutrition
-
Aspergillus saitoi and the extracellular protease play important roles in japanese food production, overview
nutrition
-
Aspergillus sojae and the extracellular protease play important roles in japanese food production, overview
nutrition
-
Aspergillus saitoi and the extracellular protease play important roles in japanese food production, overview
-
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LINKS TO OTHER DATABASES (specific for EC-Number 3.4.23.18)
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