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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 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 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 induces asthma in mice
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 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
-
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)
-
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
-
additional information
-
analysis of N-terminal amino acid sequence indicated that the purified enzyme is an acid protease
-
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PEPA_TRIVH
Trichophyton verrucosum (strain HKI 0517)
403
0
43002
Swiss-Prot
Secretory Pathway (Reliability: 2)
PEPA_ASPFC
Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163)
395
1
41613
Swiss-Prot
Secretory Pathway (Reliability: 2)
PEPA_ASPFN
Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167)
404
0
42313
Swiss-Prot
Secretory Pathway (Reliability: 3)
PEPA_ASPFU
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
395
1
41613
Swiss-Prot
Secretory Pathway (Reliability: 2)
PEPA_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
394
0
41276
Swiss-Prot
Secretory Pathway (Reliability: 2)
PEPA_ASPNG
394
0
41230
Swiss-Prot
Secretory Pathway (Reliability: 2)
PEPA_ASPOR
Aspergillus oryzae (strain ATCC 42149 / RIB 40)
404
0
42313
Swiss-Prot
Secretory Pathway (Reliability: 3)
PEPA_ASPOZ
390
0
40551
Swiss-Prot
Secretory Pathway (Reliability: 1)
PEPA_ASPPE
390
0
40623
Swiss-Prot
Secretory Pathway (Reliability: 1)
PEPA_ASPPH
394
0
41298
Swiss-Prot
Secretory Pathway (Reliability: 2)
PEPA_EMENI
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
386
0
41194
Swiss-Prot
Secretory Pathway (Reliability: 3)
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
Secretory Pathway (Reliability: 2)
PEPA_ARTBC
Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371)
403
0
42980
Swiss-Prot
Secretory Pathway (Reliability: 2)
PEPA_ASPAW
394
0
41177
Swiss-Prot
Secretory Pathway (Reliability: 2)
PEPA_ASPCL
Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107)
394
0
40934
Swiss-Prot
Secretory Pathway (Reliability: 3)
A0A4Y5UUB5_9EURO
424
0
44493
TrEMBL
Secretory Pathway (Reliability: 1)
A0A499RIG5_9EURO
394
0
41456
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1S9DPK6_ASPOZ
425
0
45007
TrEMBL
Secretory Pathway (Reliability: 3)
I8A3B4_ASPO3
Aspergillus oryzae (strain 3.042)
400
0
43033
TrEMBL
Secretory Pathway (Reliability: 3)
A0A364M9I1_ASPFL
404
0
42313
TrEMBL
Secretory Pathway (Reliability: 3)
G3XTH5_ASPNA
Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7)
426
0
46730
TrEMBL
other Location (Reliability: 5)
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
Secretory Pathway (Reliability: 2)
A0A1L9X0G5_ASPA1
Aspergillus aculeatus (strain ATCC 16872 / CBS 172.66 / WB 5094)
399
0
41383
TrEMBL
Secretory Pathway (Reliability: 1)
A0A7G5JCE1_ASPFN
Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167)
404
0
42313
TrEMBL
Secretory Pathway (Reliability: 3)
A0A5N6H542_ASPFL
423
0
46572
TrEMBL
other Location (Reliability: 2)
A0A1L9WLX8_ASPA1
Aspergillus aculeatus (strain ATCC 16872 / CBS 172.66 / WB 5094)
426
0
44962
TrEMBL
Secretory Pathway (Reliability: 2)
A0A5N6YWR5_9EURO
420
0
46097
TrEMBL
other Location (Reliability: 3)
A2Q7E3_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
393
0
42757
TrEMBL
other Location (Reliability: 5)
A0A254UDY8_ASPNG
424
0
44946
TrEMBL
Secretory Pathway (Reliability: 2)
A0A7U2MUA0_ASPFL
400
0
43032
TrEMBL
Secretory Pathway (Reliability: 3)
A0A117E4L6_ASPNG
426
0
46685
TrEMBL
other Location (Reliability: 5)
A0A5N5XIG8_9EURO
420
0
45919
TrEMBL
other Location (Reliability: 3)
I7ZVS3_ASPO3
Aspergillus oryzae (strain 3.042)
424
0
45003
TrEMBL
Secretory Pathway (Reliability: 3)
A0A364MBI4_ASPFL
396
0
42704
TrEMBL
Secretory Pathway (Reliability: 3)
A0A221SE19_ASPFL
68
0
7097
TrEMBL
other Location (Reliability: 1)
I8IK46_ASPO3
Aspergillus oryzae (strain 3.042)
420
0
46261
TrEMBL
other Location (Reliability: 2)
A0A7G5J640_ASPFN
Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167)
399
0
42930
TrEMBL
Secretory Pathway (Reliability: 3)
A0A2I2GE27_9EURO
422
0
44948
TrEMBL
Secretory Pathway (Reliability: 2)
B8MBN5_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
309
0
32772
TrEMBL
Mitochondrion (Reliability: 5)
B8MBN5_TALSN
309
0
32772
TrEMBL
Mitochondrion (Reliability: 5)
A0A1S9D891_ASPOZ
404
0
42313
TrEMBL
Secretory Pathway (Reliability: 3)
A0A2P2HUS6_ASPFA
Aspergillus flavus (strain ATCC MYA-384 / AF70)
404
0
42313
TrEMBL
Secretory Pathway (Reliability: 3)
Q2UCB1_ASPOR
Aspergillus oryzae (strain ATCC 42149 / RIB 40)
399
0
42917
TrEMBL
Secretory Pathway (Reliability: 3)
A0A1S9D5E4_ASPOZ
420
0
46261
TrEMBL
other Location (Reliability: 2)
A0A2P2HEM5_ASPFA
Aspergillus flavus (strain ATCC MYA-384 / AF70)
399
0
42903
TrEMBL
Secretory Pathway (Reliability: 3)
A1YWA4_ASPNG
394
0
41982
TrEMBL
Secretory Pathway (Reliability: 2)
A0A5N5WYH0_9EURO
425
0
44854
TrEMBL
Secretory Pathway (Reliability: 2)
A0A318ZSD5_ASPLB
Aspergillus lacticoffeatus (strain CBS 101883)
394
0
41277
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2I2FUQ3_9EURO
395
0
41631
TrEMBL
Secretory Pathway (Reliability: 4)
A0A2P2H153_ASPFA
Aspergillus flavus (strain ATCC MYA-384 / AF70)
420
0
46253
TrEMBL
other Location (Reliability: 2)
A0A6G9IW31_9HELO
Bispora sp
407
0
42021
TrEMBL
Secretory Pathway (Reliability: 1)
A0A254UAL0_ASPNG
394
0
41277
TrEMBL
Secretory Pathway (Reliability: 2)
A0A7G5K4F3_ASPFL
425
0
45023
TrEMBL
Secretory Pathway (Reliability: 3)
A0A100IK58_ASPNG
394
0
41298
TrEMBL
Secretory Pathway (Reliability: 2)
B8NS01_ASPFN
Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167)
420
0
46227
TrEMBL
other Location (Reliability: 2)
A1YWA5_ASPNG
426
0
46730
TrEMBL
other Location (Reliability: 5)
Q2UUQ0_ASPOR
Aspergillus oryzae (strain ATCC 42149 / RIB 40)
420
0
46227
TrEMBL
other Location (Reliability: 2)
A0A1L9X7W0_ASPA1
Aspergillus aculeatus (strain ATCC 16872 / CBS 172.66 / WB 5094)
420
0
45679
TrEMBL
Mitochondrion (Reliability: 5)
B8N6H9_ASPFN
Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167)
425
0
45023
TrEMBL
Secretory Pathway (Reliability: 3)
A0A319AIJ4_ASPLB
Aspergillus lacticoffeatus (strain CBS 101883)
424
0
44946
TrEMBL
Secretory Pathway (Reliability: 2)
A0A5M3YYM7_ASPTE
424
0
45330
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0F4Z587_TALEM
919
0
98506
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0F4YKI8_TALEM
395
0
41769
TrEMBL
Secretory Pathway (Reliability: 2)
A0A364M0L0_ASPFL
425
0
45007
TrEMBL
Secretory Pathway (Reliability: 3)
Q0CJF2_ASPTN
Aspergillus terreus (strain NIH 2624 / FGSC A1156)
302
0
31681
TrEMBL
Secretory Pathway (Reliability: 3)
A0A5M3Z588_ASPTE
395
0
41720
TrEMBL
Secretory Pathway (Reliability: 3)
B8N6F5_ASPFN
Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167)
400
0
43032
TrEMBL
Secretory Pathway (Reliability: 3)
A0A3M7JJ18_ASPFL
420
0
46227
TrEMBL
other Location (Reliability: 2)
Q2UDE1_ASPOR
Aspergillus oryzae (strain ATCC 42149 / RIB 40)
425
0
45007
TrEMBL
Secretory Pathway (Reliability: 3)
A0A5N5XE11_9EURO
404
0
42564
TrEMBL
Secretory Pathway (Reliability: 3)
A0A5N6Z6R3_9EURO
425
0
45065
TrEMBL
Secretory Pathway (Reliability: 4)
A0A076JCD5_ASPFL
68
0
6912
TrEMBL
other Location (Reliability: 1)
A0A5N6GZX9_ASPFL
400
0
43033
TrEMBL
Secretory Pathway (Reliability: 3)
G3XWX0_ASPNA
Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7)
424
0
44946
TrEMBL
Secretory Pathway (Reliability: 2)
A0A370CEQ0_ASPNG
394
0
41276
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1S9DQK4_ASPOZ
396
0
42676
TrEMBL
Secretory Pathway (Reliability: 3)
A0A5N6TMS0_9EURO
424
0
44987
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0F4YZQ0_TALEM
397
0
41375
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2P2HE65_ASPFA
Aspergillus flavus (strain ATCC MYA-384 / AF70)
425
0
45007
TrEMBL
Secretory Pathway (Reliability: 3)
Q8X1C9_TALEM
421
1
44683
TrEMBL
Secretory Pathway (Reliability: 2)
A2R613_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
381
0
40195
TrEMBL
Mitochondrion (Reliability: 5)
A0A319BA60_ASPLB
Aspergillus lacticoffeatus (strain CBS 101883)
426
0
46730
TrEMBL
other Location (Reliability: 5)
A0A370C2U2_ASPNG
424
0
44946
TrEMBL
Secretory Pathway (Reliability: 2)
A0A5N6ZGB2_9EURO
400
0
42269
TrEMBL
Secretory Pathway (Reliability: 3)
Q0CVD5_ASPTN
Aspergillus terreus (strain NIH 2624 / FGSC A1156)
424
0
45246
TrEMBL
Secretory Pathway (Reliability: 2)
A0A370BZ66_ASPNG
426
0
46730
TrEMBL
other Location (Reliability: 5)
A0A5N6U8K9_9EURO
402
0
41980
TrEMBL
Secretory Pathway (Reliability: 3)
I8A4M3_ASPO3
Aspergillus oryzae (strain 3.042)
404
0
42313
TrEMBL
Secretory Pathway (Reliability: 3)
AL15_ASPFU
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
152
0
15944
Swiss-Prot
-
Q334I5_TRIHA
386
0
39564
TrEMBL
-
Q2WBH2_HYPJE
407
0
42688
TrEMBL
-
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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 luchuensis
-
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 phoenicis, Aspergillus niger B
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 (Q06902), Aspergillus oryzae, 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 luchuensis, Aspergillus niger, Aspergillus oryzae, Aspergillus phoenicis, Aspergillus sojae, Aspergillus phoenicis R-3813
-
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 (Q06902), Aspergillus oryzae, Aspergillus oryzae RIB 40 (Q06902), Aspergillus oryzae ATCC 42149 (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