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angiotensin + H2O
?
-
cleavage site: Tyr-Ile, not His-Pro, Aspergillus oryzae enzyme, cleavage specificity compared to pepsin and cathepsin D
-
-
-
angiotensin II + H2O
?
-
cleavage site: Tyr4-Ile5
-
-
-
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 + H2O
Benzyloxycarbonyl-Lys + Ala-Ala
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 + H2O
Benzyloxycarbonyl-Lys + Leu-Ala
Benzyloxycarbonyl-Lys-Leu-Ala-Ala + H2O
Benzyloxycarbonyl-Lys + Leu-Ala-Ala
-
-
-
-
Benzyloxycarbonyl-Lys-Phe-Ala + H2O
Benzyloxycarbonyl-Lys + Phe-Ala
Chymotrypsinogen + H2O
Pi-Chymotrypsin
chymotrypsinogen A + H2O
chymotrypsin + peptide fragment
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
-
-
?
DRVYIHPFHLLVYS + 3 H2O
DRVY + Ile-His + PFHLL + VYS
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
-
-
?
Gelatin + H2O
?
-
-
-
-
?
milk protein + H2O
?
-
-
-
?
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
-
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
-
?
resorufin-labelled casein + H2O
?
soy protein + H2O
?
-
-
-
?
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
-
-
?
additional information
?
-
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
-
-
-
-
casein + H2O

?
-
-
-
-
-
casein + H2O
?
-
milk casein
-
-
?
casein + H2O
?
-
milk casein
-
-
?
casein + H2O
?
-
highest activity
-
-
?
casein + H2O
?
-
highest activity
-
-
?
Chymotrypsinogen + H2O

Pi-Chymotrypsin
-
cleavage site: Arg15-Ile16
-
-
Chymotrypsinogen + H2O
Pi-Chymotrypsin
-
bovine chymotrypsinogen
-
-
Chymotrypsinogen + H2O
Pi-Chymotrypsin
-
-
-
-
-
Chymotrypsinogen + H2O
Pi-Chymotrypsin
-
-
-
-
-
chymotrypsinogen A + H2O

chymotrypsin + peptide fragment
-
activation
-
-
?
chymotrypsinogen A + H2O
chymotrypsin + peptide fragment
-
activation
-
-
?
Cytochrome c + H2O

?
-
-
-
-
-
Cytochrome c + H2O
?
-
from horse heart
-
-
-
Cytochrome c + H2O
?
-
-
-
-
-
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
-
-
?
Hemoglobin + H2O

?
-
-
-
-
-
Hemoglobin + H2O
?
-
best substrate
-
-
-
Hemoglobin + H2O
?
-
-
-
-
-
Hemoglobin + H2O
?
-
-
-
-
-
Hemoglobin + H2O
?
-
urea-denatured hemoglobin
-
-
-
Hemoglobin + H2O
?
-
urea-denatured hemoglobin
-
-
-
Hemoglobin + H2O
?
-
-
-
-
-
Myoglobin + H2O

?
-
-
-
-
?
Myoglobin + H2O
?
-
-
-
-
?
resorufin-labelled casein + H2O

?
-
-
-
?
resorufin-labelled casein + H2O
?
-
-
-
?
Trypsinogen + H2O

?
-
-
-
-
-
Trypsinogen + H2O
?
-
-
-
-
-
Trypsinogen + H2O
?
-
-
-
-
-
Trypsinogen + H2O
?
-
bovine (pancreatic)
-
-
-
Trypsinogen + H2O
?
-
better substrate than chymotrypsinogen
-
-
-
Trypsinogen + H2O
?
-
bovine (trypsinogen)
-
-
-
Trypsinogen + H2O
?
-
bovine (pancreatic)
-
-
-
Trypsinogen + H2O
?
-
bovine (trypsinogen)
-
-
-
Trypsinogen + H2O
?
-
-
-
-
-
Trypsinogen + H2O
?
-
cleaves Lys-Ile and liberates hexapeptide
-
-
-
Trypsinogen + H2O
?
-
cleavage site: Lys6-Ile7
-
-
-
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
?
-
-
specificity
-
-
-
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
?
-
-
specificity
-
-
-
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
?
-
-
specificity
-
-
-
additional information
?
-
-
specificity
-
-
-
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 milk clotting activity
-
-
-
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
?
-
-
no milk clotting activity
-
-
-
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 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 propeptide is necessary for catalytic activity
-
-
-
additional information
?
-
-
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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1,2-epoxy-3-(4-nitrophenoxy)propane
DAN
-
91.7% residual activity at 5 mM
Diazoacetyl-DL-norleucine methyl ester
dithiothreitol
-
90.1% residual activity at 5 mM
DL-1-Diazo-3-tosylamido-2-heptanone
-
in the presence of Cu2+
EDTA
-
87.3% residual activity at 5 mM
Fe3+
-
81.1% residual activity at 10 mM
Hg2+
-
74.8% residual activity at 10 mM
IAA
-
94.8% residual activity at 5 mM
K+
-
97.4% residual activity at 10 mM
L-1-Diazo-3-tosylamido-4-phenyl-2-butanone
-
in the presence of Cu2+
Mn2+
-
85.9% residual activity at 10 mM
N-ethylmaleimide
-
88.8% residual activity at 5 mM
Na+
-
92.54% residual activity at 10 mM
NaN3
-
78% residual activity at 5 mM
NBS
-
49.7% residual activity at 5 mM
pepstatin A
specific inhibition of the mature enzyme
phenylmethylsulfonyl fluoride
-
16.3% residual activity at 5 mM
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)
-
sodium perborate
-
92.1% residual activity after 3 h at 1% (v/v)
Streptomyces pepsin inhibitor
-
-
-
TLCK
-
93.3% residual activity at 5 mM
Urea
-
95.5% residual activity at 5 mM
Zn2+
-
89.1% residual activity at 10 mM
1,2-epoxy-3-(4-nitrophenoxy)propane

-
pH-profile
1,2-epoxy-3-(4-nitrophenoxy)propane
-
pH-profile
1,2-epoxy-3-(4-nitrophenoxy)propane
-
the reaction is markedly inhibited by pepstatin
1,2-epoxy-3-(4-nitrophenoxy)propane
-
pH-profile
1,2-epoxy-3-(4-nitrophenoxy)propane
-
not
Diazoacetyl-DL-norleucine methyl ester

-
-
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
N-bromosuccinimide

-
not
pepstatin

-
kinetics
pepstatin
complete inhibition at 10 mM
SDS

-
-
additional information

-
diisopropyl phosphofluoridate; EDTA; no inhibition by p-chloromercuribenzene sulfonate, AgNO3, 2-mercaptoethanol, PMSF
-
additional information
-
diisopropyl phosphofluoridate
-
additional information
-
diisopropyl phosphofluoridate; EDTA; HgCl2, NaF, FeCl3, FeCl2, CoCl2, MgCl2, CaCl2, ZnSO4; monoiodoacetate, 1,10-phenanthroline, 6-aminohexanoate; PCMB
-
additional information
-
soybean trypsin inhibitor; Triton X-100
-
additional information
-
diisopropyl phosphofluoridate; monoiodoacetate, 1,10-phenanthroline, 6-aminohexanoate; PCMB
-
additional information
-
not inhibited by H2O2
-
additional information
-
not inhibited by Fe2+ and Cu2+
-
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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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 enzyme induces asthma in mice
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-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
-
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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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.
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