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Information on EC 3.4.23.18 - Aspergillopepsin I
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3.4.23.18 Aspergillopepsin ISpecify your search results
Word Map
- 3.4.23.18
- cathepsins
- pepstatin
- proteinases
- lysosomal
- hemoglobin
- alzheimer
- candida
- renin
- plasmodium
-
amyloid
- albicans
- zymogen
- pepsinogen
- malaria
- falciparum
- beta-secretase
-
plasmepsins
- flap
-
subsite
- chymosin
- mucor
-
pregnancy-associated
- gamma-secretase
-
cheese
- leupeptin
- d-like
- rhizopus
-
beta-site
- napsins
- beta-amyloid
-
procathepsin
- angiotensinogen
-
scissile
-
milk-clotting
- polyproteins
-
aspartyl
-
peptidomimetic
- abeta
- proenzyme
- rhizomucor
-
hookworm
-
isostere
- prosegment
- nutrition
- miehei
- cynara
- parasitica
- bace-1
- boophilus
-
autoprocessing
- microplus
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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
Synonyms
A. protease, Acid protease, ACP, AOAP, AP, APP, Asp f 13, Asp f 15, aspartic protease, aspartic protease P6281, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Acid protease
ACP
Asp f 13
Asp f 15
aspartic protease
aspartic protease P6281
Aspartic proteinase
Aspergillopepsin A
aspergillopepsin O
Aspergillopeptidase A
Aspergillus acid protease
-
-
-
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Aspergillus acid proteinase
-
-
-
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Aspergillus aspartic proteinase
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-
-
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Aspergillus awamori acid proteinase
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-
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Aspergillus carboxyl proteinase
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-
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Aspergillus niger acid proteinase
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-
-
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Aspergillus saitoi acid proteinase
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-
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Avamorin
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-
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Carboxyl proteinase
-
-
-
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Denapsin
-
-
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Denapsin XP 271
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-
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EC 3.4.23.6
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-
formerly
-
extracellular aspartic protease
PepA
PEPO
Pepsin-type aspartic proteinase
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-
-
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Proctase
-
-
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Proctase B
Proctase P
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-
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Proteinase B
Proteinase, Aspergillus acid
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-
-
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Proteinase, Aspergillus awamori acid
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-
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Proteinase, Aspergillus kawachii aspartic
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-
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Proteinase, Aspergillus saitoi acid
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-
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Sumizyme AP
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-
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Trypsinogen kinase
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-
-
-
additional information
Aspergillopepsin A
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-
-
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Proctase B
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-
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Proteinase B
-
-
-
-
additional information
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the enzyme belongs to the A1 peptidase family
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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
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-
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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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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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-
-
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CAS REGISTRY NUMBER
COMMENTARY
9025-49-4
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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
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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
-
-
-
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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
-
-
-
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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
-
-
-
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Dnp-Ala-Ala-Phe-Phe-Ala-Arg-NH2 + H2O
Dnp-Ala-Ala-Phe + Phe-Ala-Arg-NH2
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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
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-
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
FVNQHLCGSH + LVEA + Leu + Tyr + LVCGERGF + FYTPKA
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substrate is the oxidized insulin B chain, cleavage site specificity, overview
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-
?
N2-acetyl-D-arginyl-L-lysyl-L-isoleucyl-N-[(2S)-1-[(2S)-2-[[(1R)-4-carbamimidamido-1-carboxybutyl]carbamoyl]pyrrolidin-1-yl]-4-[methyl[(4-nitrophenoxy)carbonyl]amino]-1-oxobutan-2-yl]-L-argininamide + H2O
N2-acetyl-D-arginyl-L-lysyl-L-isoleucyl-L-arginine + 1-[(2S)-2-amino-4-[methyl[(4-nitrophenoxy)carbonyl]amino]butanoyl]-L-prolyl-D-argininamide
-
-
-
-
ir
Oxidized insulin B-chain + H2O
Hydrolyzed insulin B-chain
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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
?
-
cleavage sites: Tyr-Ile and His-Pro, Aspergillus oryzae enzyme, cleavage specificity compared to pepsin and cathepsin D
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-
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proangiotensin + H2O
DRVYIH + PFHLLVYS
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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
-
-
-
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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
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-
-
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trypsinogen + H2O
trypsin + peptide fragment
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activation by cleavage of a Lys-Pro bond
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-
?
Benzyloxycarbonyl-Lys-Ala-Ala + H2O
Benzyloxycarbonyl-Lys + Ala-Ala
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poor substrate
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Benzyloxycarbonyl-Lys-Ala-Ala + H2O
Benzyloxycarbonyl-Lys + Ala-Ala
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poor substrate
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Benzyloxycarbonyl-Lys-Leu-Ala + H2O
Benzyloxycarbonyl-Lys + Leu-Ala
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-
-
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Benzyloxycarbonyl-Lys-Leu-Ala + H2O
Benzyloxycarbonyl-Lys + Leu-Ala
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-
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Benzyloxycarbonyl-Lys-Leu-Ala + H2O
Benzyloxycarbonyl-Lys + Leu-Ala
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-
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Benzyloxycarbonyl-Lys-Phe-Ala + H2O
Benzyloxycarbonyl-Lys + Phe-Ala
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-
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Benzyloxycarbonyl-Lys-Phe-Ala + H2O
Benzyloxycarbonyl-Lys + Phe-Ala
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-
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Benzyloxycarbonyl-Lys-Phe-Ala + H2O
Benzyloxycarbonyl-Lys + Phe-Ala
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Chymotrypsinogen + H2O
Pi-Chymotrypsin
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cleavage site: Arg15-Ile16
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chymotrypsinogen A + H2O
chymotrypsin + peptide fragment
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activation
-
-
?
chymotrypsinogen A + H2O
chymotrypsin + peptide fragment
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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
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-
?
Trypsinogen + H2O
?
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cleaves Lys-Ile and liberates hexapeptide
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-
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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
?
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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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-
-
additional information
?
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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
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-
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additional information
?
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the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
-
-
-
additional information
?
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-
no hydrolysis of benzyloxycarbonyl-Lys-Gly-Ala, benzyloxycarbonyl-Lys-(D)-Leu-Ala
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-
-
additional information
?
-
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the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
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-
additional information
?
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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
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-
-
additional information
?
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no hydrolysis of benzyloxycarbonyl-Lys-Gly-Ala, benzyloxycarbonyl-Lys-(D)-Leu-Ala
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-
-
additional information
?
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the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
-
-
-
additional information
?
-
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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
?
-
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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
?
-
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the enzyme efficiently decolorises red-pigmented proteins during dried bonito fermentation. The enzyme is also able to decolorise flaked, dried bonito and to bleach a blood-stained cloth
-
-
-
additional information
?
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the propeptide is necessary for catalytic activity
-
-
-
additional information
?
-
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the enzyme efficiently decolorises red-pigmented proteins during dried bonito fermentation. The enzyme is also able to decolorise flaked, dried bonito and to bleach a blood-stained cloth
-
-
-
additional information
?
-
-
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
-
-
-
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NATURAL SUBSTRATE
NATURAL 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
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
Ca2+
Mg2+
additional information
additional information
-
no activation by HgCl2, NaF, FeCl3, FeCl2, CoCl2, MgCl2, CaCl2, ZnSO4
additional information
Fe2+ and Zn2+ have negligible effect on the enzyme activity
additional information
-
Fe2+ and Zn2+ have negligible effect on the enzyme activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
polyoxyethylene lauryl ether
-
88.7% residual activity after 3 h at 1% (v/v)
-
sodium laurylbenzenesulfonic acid
-
5.5% residual activity after 3 h at 1% (v/v)
-
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
-
additional information
EDTA has a negligible effect on the enzyme activity
-
additional information
-
EDTA has a negligible effect on the enzyme activity
-
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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
-
additional information
-
the enzyme activity remains unaltered in the presence of H2O2 and NaClO
-
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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
242
purified enzyme, pH 3.0, temperature not specified in the publication
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
2 - 6
about 5% activity at pH 2.0, 100% activity at pH 2.5, about 95% activity at pH 3.0, about 60% activity at pH 3.5, about 50% activity at pH 4.0, about 15% activity at pH 5.0, about 3% activity at pH 6.0
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
50
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
Taka-diastase, crude Aspergillus oryzae powder preparation
brenda
-
extracellular enzyme; Taka-diastase, crude Aspergillus oryzae powder preparation
brenda
the enzyme is isolated from an Amano protease preparation from Aspergillus oryzae, enzyme AcP is purified from Biozyme A
brenda
-
extracellular enzyme; Taka-diastase, crude Aspergillus oryzae powder preparation
-
brenda
-
the enzyme is isolated from an Amano protease preparation from Aspergillus oryzae, enzyme AcP is purified from Biozyme A
-
brenda
-
the enzyme is isolated from an Amano protease preparation from Aspergillus oryzae, enzyme AcP is purified from Biozyme A
-
brenda
enzyme synthesis during formation of germ tubes, the pH droops during germination from pH 5.5 to pH 3.5
brenda
-
enzyme synthesis during formation of germ tubes, the pH droops during germination from pH 5.5 to pH 3.5
-
brenda
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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
brenda
-
2 forms: extracellular and cytoplasmic, the cytoplasmic isozymes are immunologically related to extracellular isozyme A2
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
additional information
physiological function
Aspergillus fumigatus-secreted allergen proteases, Asp f 5 and Asp f 13, are important for recruitment of inflammatory cells and remodelling of the airways in mice. The enzymes are important for initiation and progression of allergic asthma
physiological function
the enzyme significantly inhibits spore germination and growth of plant and animal pathogenic fungi such as Botrytis cinerea, Mucor circinelloides, Aspergillus fumigatus, Aspergillus flavus, Rhizoctonia solani, and Candida albicans. The enzyme efficiently damages the cell wall of Botrytis cinerea. In addition, the protease significantly inhibits the development of grey mold that causes rotting of apple, orange, and cucumber
physiological function
the acid protease derived from Aspergillus oryzae causes bifidogenic effect in Sprague-Dawley rats. Bifidobacterium numbers are unaffected by supplementation with purified acid protease (AcP, 0.096 g/kg) at the level equivalent to the AcP amount found in the 1-g/kg Amano protease diet. Bifidobacterium numbers in the cecum and feces, and lactate levels in the cecum are significantly elevated when rats are fed a diet containing 0.384 g/kg AcP (4fold higher amount of AcP than that used in the 1-g/kg Amano protease diet)
physiological function
Aspergillus fumigatus A1160
-
Aspergillus fumigatus-secreted allergen proteases, Asp f 5 and Asp f 13, are important for recruitment of inflammatory cells and remodelling of the airways in mice. The enzymes are important for initiation and progression of allergic asthma
-
physiological function
-
the acid protease derived from Aspergillus oryzae causes bifidogenic effect in Sprague-Dawley rats. Bifidobacterium numbers are unaffected by supplementation with purified acid protease (AcP, 0.096 g/kg) at the level equivalent to the AcP amount found in the 1-g/kg Amano protease diet. Bifidobacterium numbers in the cecum and feces, and lactate levels in the cecum are significantly elevated when rats are fed a diet containing 0.384 g/kg AcP (4fold higher amount of AcP than that used in the 1-g/kg Amano protease diet)
-
physiological function
-
the acid protease derived from Aspergillus oryzae causes bifidogenic effect in Sprague-Dawley rats. Bifidobacterium numbers are unaffected by supplementation with purified acid protease (AcP, 0.096 g/kg) at the level equivalent to the AcP amount found in the 1-g/kg Amano protease diet. Bifidobacterium numbers in the cecum and feces, and lactate levels in the cecum are significantly elevated when rats are fed a diet containing 0.384 g/kg AcP (4fold higher amount of AcP than that used in the 1-g/kg Amano protease diet)
-
physiological function
Trichoderma harzianum GIM 3.442
-
the enzyme significantly inhibits spore germination and growth of plant and animal pathogenic fungi such as Botrytis cinerea, Mucor circinelloides, Aspergillus fumigatus, Aspergillus flavus, Rhizoctonia solani, and Candida albicans. The enzyme efficiently damages the cell wall of Botrytis cinerea. In addition, the protease significantly inhibits the development of grey mold that causes rotting of apple, orange, and cucumber
-
additional information
analysis of N-terminal amino acid sequence indicated that the purified enzyme is an acid protease
additional information
-
analysis of N-terminal amino acid sequence indicated that the purified enzyme is an acid protease
-
additional information
-
analysis of N-terminal amino acid sequence indicated that the purified enzyme is an acid protease
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
PEPA_TRIVH
Trichophyton verrucosum (strain HKI 0517)
403
0
43002
Swiss-Prot
PEPA_ARTBC
Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371)
403
0
42980
Swiss-Prot
PEPA_ASPCL
Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
394
0
40934
Swiss-Prot
PEPA_ASPFC
Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163)
395
1
41613
Swiss-Prot
PEPA_ASPFN
Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167)
404
0
42313
Swiss-Prot
PEPA_ASPFU
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
395
1
41613
Swiss-Prot
PEPA_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
394
0
41276
Swiss-Prot
PEPA_ASPOR
Aspergillus oryzae (strain ATCC 42149 / RIB 40)
404
0
42313
Swiss-Prot
PEPA_EMENI
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
386
0
41194
Swiss-Prot
PEPA_NEOFI
Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181)
395
1
41574
Swiss-Prot
A2Q7E3_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
393
0
42757
TrEMBL
G3XNE5_ASPNA
Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7)
394
0
41277
TrEMBL
B8MBN5_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
309
0
32772
TrEMBL
A2R613_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
381
0
40195
TrEMBL
AL15_ASPFU
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
152
0
15944
Swiss-Prot
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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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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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
x * 42000, proenzyme, SDS-PAGE, x * 41000, mature enzyme, SDS-PAGE
?
-
x * 42000, proenzyme, SDS-PAGE, x * 41000, mature enzyme, SDS-PAGE; x * 44000, SDS-PAGE
-
?
-
x * 38000, mature enzyme, SDS-PAGE; x * 47000, proenzyme, SDS-PAGE
?
x * 55000, catalytically active enzyme with propeptide, SDS-PAGE
?
-
x * 38000, mature enzyme, SDS-PAGE; x * 47000, proenzyme, 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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
gene disruption leads to 85% reduced extracellular proteolytic activity
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.5 - 6
5 - 8
-
the protease is relatively stable at pH 5.0, except in buffer containing sodium laurylbenzenesulfonic acid. However, at pH 8.0, whether in the absence or presence of reagents for 1 h, it loses almost all activity
754494
8 - 12
-
the protease demonstrates excellent stability at pH range 8.0-12.0 for 30 min. The enzyme remains unaltered at pH 11.0 and 12.0 for 24 h at 28°C and a slight decrease in relative activity is seen at pH 10.0 after 24 h
752341
2.5 - 6
the enzyme is stable in the pH range of 2.5-6.0, maintaining more than 80% of its activity after 1 h of incubation. Enzymatic activity is lost after incubation at pH 10.0
753450
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 45
after incubation at 20°C for 1 h, the enzyme with propeptide retains 100% activity. 38.1°C is the melting temperature of the catalytically active enzyme with propeptide. When the temperature is over 45°C, the relative enzyme activities of the enzyme with propeptide decreases to below 40%
30
-
pH 7, drastic decrease of activity probably due to autolytic activity
30 - 50
the enzyme maintains 39.8% of its maximum activity after 5 min incubation at 50°C. The protease remains stable after 1 h of incubation at 30 and 35°C, retaining more than 70% activity
50
50 - 80
-
the enzyme is almost 100 % stable at 50°C for 24 h. Retention of full activity is seen for over 4, 2, 1 h and 30 min at 50, 60, 70 and 80°C, respectively. However, a loss in relative activity in the range of 1.3 % (50°C) to 19.6 % (at 80°C) is noted after 24 h
55
50
-
the enzyme maintains 80% activity when incubated at 50°C and pH 3.0 for 20 min
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
-
the enzyme is stable in 50 mM KCl-HCl buffer (pH 1.2 and 2.0), sodium potassium tartrate buffer (pH 3.0), 50 mM sodium acetate buffer (pH 4.0-5.0), and 50 mM sodium/potassium phosphate buffer (pH 6.0-7.0)
-
the protease is 100 % stable and compatible for 2 h at 60°C with all the detergents tested except for Super wheel, and a retention of 83.98, 85.50, 85.57, 87.14 and 89.16 % is recorded after 24 h for Super wheel, More choice, Ariel, Henko and Surf excel, respectively
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is 100 % stable in the presence of bleaching and oxidizing agents
-
752341
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4, 7 and 9% of the enzyme's initial activity are lost after 40 days at 4, 28 and -20°C, respectively
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cytoplasmic enzyme: partial; several isoforms (cytoplasmic F1 and F2); several isoforms (extracellular A1 and A2)
-
Ni2+-Sepharose column chromatography and glutathione Sepharose column chromatography
recombinant enzyme from Escherichia coli after solubilization from inclusion bodies by ion exchange chromatography to homogeneity
-
the enzyme is purified by 46fold from an Amano protease preparation from Aspergillus oryzae
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, phylogenetic analysis of Aspergillus
expressed in Pichia pastoris strain GS115
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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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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lu, J.F.; Inoue, H.; Kimura, T.; Makabe, O.; Takahashi, K.
Molecular cloning of a cDNA for proctase B from Aspergillus niger var. macrosporus and sequence comparison with other aspergillopepsins I
Biosci. Biotechnol. Biochem.
59
954-955
1995
Aspergillus awamori, Aspergillus niger, Aspergillus phoenicis
brenda
Takeuchi, M.; Ueno, Y.; Ichishima, E.
Fluorogenic substrate of Aspergillus aspartic proteinase
Agric. Biol. Chem.
52
1279-1280
1988
Aspergillus phoenicis
-
brenda
Tello-Solis, S.R.; Hernandez-Arana, A.
Effect of irreversibility on the thermodynamic characterization of the thermal denaturation of Aspergillus saitoi acid proteinase
Biochem. J.
311
969-974
1995
Aspergillus phoenicis
brenda
Majima, E.; Oda, K.; Murao, S.; Ichishima, E.
Comparative study on the specificities of several fungal aspartic and acidic proteinases towards the tetradecapeptide of a renin substrate
Agric. Biol. Chem.
52
787-793
1988
Aspergillus oryzae, Aspergillus phoenicis, Aspergillus sojae
-
brenda
Yagi, F.; Fan, J.; Tadera, K.; Kobayashi, A.
Purification and characterization of carboxyl proteinase from Aspergillus kawachii
Agric. Biol. Chem.
50
1029-1033
1986
Aspergillus kawachii
-
brenda
Bhumibhamon, O.
Precipitation and characteristics of acid protease of Aspergillus phoenicis produced with and without surfactant in the culture medium
Thai J. Agric. Sci.
15
157-172
1982
Aspergillus phoenicis
-
brenda
Panneerselvam, M.; Dhar, S.C.
Physico-chemical properties of the acid proteinase from A. fumigatus
Ital. J. Biochem.
30
63-74
1981
Aspergillus fumigatus
brenda
Bhumibhamon, O.
Some characreristics of the acid protease of Aspergillus awamori
Thai J. Agric. Sci.
12
27-33
1979
Aspergillus awamori
-
brenda
Ichishima, E.
Purification and mode of assay for acid proteinase of Aspergillus saitoi
Methods Enzymol.
19
397-406
1970
Aspergillus phoenicis, Aspergillus phoenicis R-3813
-
brenda
Kovaleva, G.G.; Shimanskaya, M.P.; Stepanov, V.M.
The site of diazoacetyl inhibitor attachment to acid proteinase of Aspergillus awamori--an analog of penicillopepsin and pepsin
Biochem. Biophys. Res. Commun.
49
1075-1081
1972
Aspergillus awamori
brenda
Morihara, K.; Oka, T.
Comparative specificity of microbial acid proteinases for synthetic peptides. 3. Relationship with their trypsinogen activating ability
Arch. Biochem. Biophys.
157
561-572
1973
Aspergillus niger, Aspergillus niger B, Aspergillus phoenicis
brenda
Davidson, R.; Gertler, A.; Hofmann, T.
Aspergillus oryzae acid proteinase. Purification and properties, and formation of pi-chymotrypsin
Biochem. J.
147
45-53
1975
Aspergillus oryzae
brenda
Takahashi, K.; Chang, W.J.
The structure and function of acid proteases. V. Comparative studies on the specific inhibition of acid proteases by diazoacetyl-DL-norleucine methyl ester, 1,2-epoxy-3-(p-nitrophenoxy) propane and pepstatin
J. Biochem.
80
497-506
1976
Aspergillus niger, Aspergillus phoenicis
brenda
Tsujita, Y.; Endo, A.
Purification and characterization of the two molecular forms of Aspergillus oryzae acid protease
Biochim. Biophys. Acta
445
194-204
1976
Aspergillus oryzae
brenda
Tsujita, Y.; Endo, A.
Presence and partial characterization of internal acid protease of Aspergillus oryzae
Appl. Environ. Microbiol.
36
237-242
1978
Aspergillus oryzae, Aspergillus oryzae 365-U-64-1
brenda
Tanaka, N.; Takeuchi, M.; Ichishima, E.
Purification of an acid proteinase from Aspergillus saitoi and determination of peptide bond specificity
Biochim. Biophys. Acta
485
406-416
1977
Aspergillus phoenicis
brenda
Chang, W.Y.; Horiuchi, S.; Takahashi, K.; Yamasaki, M.; Yamada, Y.
The structure and function of acid proteases. VI. Effects of acid protease-specific inhibitors on the acid proteases from Aspergillus niger var. macrosporus
J. Biochem.
80
975-981
1976
Aspergillus niger
brenda
Iio, K.; Yamasaki, M.
Specificity of acid proteinase A from Aspergillus niger var. macrosporus towards B-chain of performic acid oxidized bovine insulin
Biochim. Biophys. Acta
429
912-924
1976
Aspergillus niger
brenda
Krishnan, S.; Vijayalakshmi, M.A.
Purification of an acid protease and a serine carboxypeptidase from Aspergillus niger using metal-chelate affinity chromatography
J. Chromatogr.
329
165-170
1985
Aspergillus niger
brenda
Tsujita, Y.; Endo, A.
Purification and characterization of the two molecular forms of membrane acid protease from Aspergillus oryzae
Eur. J. Biochem.
84
347-353
1978
Aspergillus oryzae
brenda
Cho, S.W.; Kim, N-j.; Choi, M.U.; Shin, W.
Structure of aspergillopepsin I from Aspergillus phoenicis: variations of the S1'-S2 subsite in aspartic proteinases
Acta Crystallogr. Sect. D
57
948-956
2001
Aspergillus phoenicis
brenda
Kamitori, S.; Ohtaki, A.; Ino, H.; Takeuchi, M.
Crystal structures of Aspergillus oryzae aspartic proteinase and its complex with an inhibitor pepstatin at 1.9A resolution
J. Mol. Biol.
326
1503-1511
2003
Aspergillus oryzae
brenda
Zhu, L.Y.; Nguyen, C.H.; Sato, T.; Takeuchi, M.
Analysis of secreted proteins during conidial germination of Aspergillus oryzae RIB40
Biosci. Biotechnol. Biochem.
68
2607-2612
2004
Aspergillus oryzae, Aspergillus oryzae (Q06902), Aspergillus oryzae RIB 40 (Q06902)
brenda
Ichishima, E.
Aspergillopepsin I
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
92-99
2004
Aspergillus awamori, Aspergillus foetidus, Aspergillus fumigatus, Aspergillus kawachii, Aspergillus niger, Aspergillus oryzae, Aspergillus phoenicis, Aspergillus phoenicis R-3813, Aspergillus sojae
-
brenda
Landbo, A.K.; Pinelo, M.; Vikbjerg, A.F.; Let, M.B.; Meyer, A.S.
Protease-assisted clarification of black currant juice: synergy with other clarifying agents and effects on the phenol content
J. Agric. Food Chem.
54
6554-6563
2006
Aspergillus niger
brenda
Niyonzima, F.N.; More, S.S.
Purification and characterization of detergent-compatible protease from Aspergillus terreus gr
3 Biotech
5
61-70
2015
Aspergillus terreus, Aspergillus terreus gr.
brenda
Namvar, S.; Warn, P.; Farnell, E.; Bromley, M.; Fraczek, M.; Bowyer, P.; Herrick, S.
Aspergillus fumigatus proteases, Asp f 5 and Asp f 13, are essential for airway inflammation and remodelling in a murine inhalation model
Clin. Exp. Allergy
45
982-993
2015
Aspergillus fumigatus (O60022), Aspergillus fumigatus A1160 (O60022)
-
brenda
Yu, X.; Ma, S.; Xu, Y.; Fu, C.; Jiang, C.; Zhou, C.
Construction and application of a novel genetically engineered Aspergillus oryzae for expressing proteases
Electron. J. Biotechnol.
29
32-38
2017
Aspergillus niger (A2R3L3)
-
brenda
Deng, J.; Huang, W.; Li, Z.; Lu, D.; Zhang, Y.; Luo, X.
Biocontrol activity of recombinant aspartic protease from Trichoderma harzianum against pathogenic fungi
Enzyme Microb. Technol.
112
35-42
2018
Trichoderma harzianum (Q334I5), Trichoderma harzianum, Trichoderma harzianum GIM 3.442 (Q334I5)
brenda
Takenaka, S.; Umeda, M.; Senba, H.; Koyama, D.; Tanaka, K.; Yoshida, K.; Doi, M.
Heterologous expression and characterisation of the Aspergillus aspartic protease involved in the hydrolysis and decolorisation of red-pigmented proteins
J. Sci. Food Agric.
97
95-101
2017
Aspergillus pseudoglaucus, Aspergillus pseudoglaucus MK82
brenda
Lim, C.; Lim, S.; Lee, B.; Cho, S.
Ginsenoside Rg1 exhibits anti-asthmatic activity in an Aspergillus protease-induced asthma model in mice
Nat. Prod. Commun.
13
415-418
2018
Aspergillus sp.
-
brenda
Yang, Y.; Iwamoto, A.; Kumrungsee, T.; Okazaki, Y.; Kuroda, M.; Yamaguchi, S.; Kato, N.
Consumption of an acid protease derived from Aspergillus oryzae causes bifidogenic effect in rats
Nutr. Res.
44
60-66
2017
Aspergillus oryzae, Aspergillus oryzae (Q06902), Aspergillus oryzae ATCC 42149 (Q06902), Aspergillus oryzae RIB 40 (Q06902)
brenda
Yoshiya, T.; Yamashita, N.; Tsuda, S.; Oohigashi, K.; Masuda, S.; Kubodera, T.; Akashi, T.
HAP-01, the first chromogenic substrate for Aspergillus oryzae acid protease
Org. Biomol. Chem.
17
776-779
2019
Aspergillus oryzae
brenda
Liu, H.; Zhang, R.; Li, L.; Zhou, L.; Xu, Y.
The high expression of Aspergillus pseudoglaucus protease in Escherichia coli for hydrolysis of soy protein and milk protein
Prep. Biochem. Biotechnol.
48
725-733
2018
Aspergillus pseudoglaucus (A0A146F0J0), Aspergillus pseudoglaucus
brenda
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