Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
angiotensin + H2O
?
-
Substrates: cleavage site: Tyr-Ile, not His-Pro, Aspergillus oryzae enzyme, cleavage specificity compared to pepsin and cathepsin D
Products: -
?
angiotensin II + H2O
?
-
Substrates: cleavage site: Tyr4-Ile5
Products: -
?
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser + H2O
?
-
Substrates: 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
Products: -
?
Benzyloxycarbonyl-Ala-Ala-Lys-Ala-Ala-Ala + H2O
Benzyloxycarbonyl-Ala-Ala-Lys + Ala-Ala-Ala
-
Substrates: best substrate
Products: -
?
Benzyloxycarbonyl-Ala-Ala-Phe-Phe 3-(4-pyridyl)propyl ester + H2O
Benzyloxycarbonyl-Ala-Ala-Phe + Phe 3-(4-pyridyl)propyl ester
-
Substrates: -
Products: -
?
Benzyloxycarbonyl-Ala-Lys-Ala-Ala-Ala + H2O
Benzyloxycarbonyl-Ala-Lys + Ala-Ala-Ala
-
Substrates: -
Products: -
?
Benzyloxycarbonyl-His-Phe-Phe ethyl ester + H2O
Benzyloxycarbonyl-His-Phe + Phe ethyl ester
-
Substrates: -
Products: -
?
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
Benzyloxycarbonyl-Lys-Leu-Ala + H2O
Benzyloxycarbonyl-Lys + Leu-Ala
Benzyloxycarbonyl-Lys-Leu-Ala-Ala + H2O
Benzyloxycarbonyl-Lys + Leu-Ala-Ala
-
Substrates: -
Products: -
?
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
-
Substrates: chromogenic synthetic peptide substrate
Products: -
?
DRVYIHPFHLLVYS + 3 H2O
DRVY + Ile-His + PFHLL + Val-Tyr-Ser
DRVYIHPFHLLVYS + 3 H2O
DRVY + Ile-His + PFHLL + VYS
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + 3 H2O
FVNQHLCGSHLVEAL + Tyr + LVCGERGF + FYTPKA
-
Substrates: substrate is the oxidized insulin B chain, primarily cleavage at Leu15-Tyr16 and Phe24-Phe25, and minor cleavage of Tyr16-Leu17, overview
Products: -
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
FVNQHLCGSH + LVEA + Leu + Tyr + LVCGERGF + FYTPKA
-
Substrates: substrate is the oxidized insulin B chain, cleavage site specificity, overview
Products: -
?
HAP-01 + H2O
?
-
Substrates: -
Products: -
?
milk protein + H2O
?
Substrates: -
Products: -
?
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
-
Substrates: -
Products: -
ir
Oxidized insulin B-chain + H2O
Hydrolyzed insulin B-chain
-
Substrates: major cleavage sites: Phe24-Phe25, Leu15-Tyr16, minor sites: Ala14-Leu15, Tyr16-Leu17, peptide bond specificity compared to other proteinases
Products: -
?
Proangiotensin + H2O
?
-
Substrates: cleavage sites: Tyr-Ile and His-Pro, Aspergillus oryzae enzyme, cleavage specificity compared to pepsin and cathepsin D
Products: -
?
proangiotensin + H2O
DRVYIH + PFHLLVYS
resorufin-labelled casein + H2O
?
soy protein + H2O
?
Substrates: -
Products: -
?
soybean isolate protein + H2O
?
tert-Butoxycarbonyl-Ile-Glu-Gly-Arg 4-methylcoumarin 7-amide + H2O
tert-Butoxycarbonyl-Ile-Glu-Gly + Arg 4-methylcoumarin 7-amide
-
Substrates: -
Products: -
?
tert-Butoxycarbonyl-Leu-Ser-Thr-Arg 4-methylcoumarin 7-amide + H2O
tert-Butoxycarbonyl-Leu-Ser-Thr + Arg 4-methylcoumarin 7-amide
-
Substrates: -
Products: -
?
trypsinogen + H2O
trypsin + peptide fragment
additional information
?
-
Benzyloxycarbonyl-Lys-Ala-Ala + H2O

Benzyloxycarbonyl-Lys + Ala-Ala
-
Substrates: poor substrate
Products: -
?
Benzyloxycarbonyl-Lys-Ala-Ala + H2O
Benzyloxycarbonyl-Lys + Ala-Ala
-
Substrates: poor substrate
Products: -
?
Benzyloxycarbonyl-Lys-Ala-Ala + H2O
Benzyloxycarbonyl-Lys + Ala-Ala
-
Substrates: poor substrate
Products: -
?
Benzyloxycarbonyl-Lys-Ala-Ala-Ala + H2O

Benzyloxycarbonyl-Lys + Ala-Ala-Ala
-
Substrates: -
Products: -
?
Benzyloxycarbonyl-Lys-Ala-Ala-Ala + H2O
Benzyloxycarbonyl-Lys + Ala-Ala-Ala
-
Substrates: -
Products: -
?
Benzyloxycarbonyl-Lys-Ala-Ala-Ala-Ala + H2O

Benzyloxycarbonyl-Lys + Ala-Ala-Ala-Ala
-
Substrates: poor substrate
Products: -
?
Benzyloxycarbonyl-Lys-Ala-Ala-Ala-Ala + H2O
Benzyloxycarbonyl-Lys + Ala-Ala-Ala-Ala
-
Substrates: poor substrate
Products: -
?
Benzyloxycarbonyl-Lys-Leu-Ala + H2O

Benzyloxycarbonyl-Lys + Leu-Ala
-
Substrates: -
Products: -
?
Benzyloxycarbonyl-Lys-Leu-Ala + H2O
Benzyloxycarbonyl-Lys + Leu-Ala
-
Substrates: -
Products: -
?
Benzyloxycarbonyl-Lys-Leu-Ala + H2O
Benzyloxycarbonyl-Lys + Leu-Ala
-
Substrates: -
Products: -
?
Benzyloxycarbonyl-Lys-Phe-Ala + H2O

Benzyloxycarbonyl-Lys + Phe-Ala
-
Substrates: -
Products: -
?
Benzyloxycarbonyl-Lys-Phe-Ala + H2O
Benzyloxycarbonyl-Lys + Phe-Ala
-
Substrates: -
Products: -
?
Benzyloxycarbonyl-Lys-Phe-Ala + H2O
Benzyloxycarbonyl-Lys + Phe-Ala
-
Substrates: -
Products: -
?
casein + H2O

?
-
Substrates: -
Products: -
?
casein + H2O
?
Substrates: -
Products: -
?
casein + H2O
?
Substrates: -
Products: -
?
casein + H2O
?
-
Substrates: -
Products: -
?
casein + H2O
?
-
Substrates: milk casein
Products: -
?
casein + H2O
?
-
Substrates: milk casein
Products: -
?
casein + H2O
?
Substrates: -
Products: -
?
casein + H2O
?
-
Substrates: highest activity
Products: -
?
casein + H2O
?
Substrates: -
Products: -
?
casein + H2O
?
Substrates: -
Products: -
?
Chymotrypsinogen + H2O

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

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

?
-
Substrates: -
Products: -
?
Cytochrome c + H2O
?
-
Substrates: from horse heart
Products: -
?
Cytochrome c + H2O
?
-
Substrates: -
Products: -
?
DRVYIHPFHLLVYS + 3 H2O

DRVY + Ile-His + PFHLL + Val-Tyr-Ser
-
Substrates: tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
Products: -
?
DRVYIHPFHLLVYS + 3 H2O
DRVY + Ile-His + PFHLL + Val-Tyr-Ser
-
Substrates: tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
Products: -
?
DRVYIHPFHLLVYS + 3 H2O

DRVY + Ile-His + PFHLL + VYS
-
Substrates: tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
Products: -
?
DRVYIHPFHLLVYS + 3 H2O
DRVY + Ile-His + PFHLL + VYS
-
Substrates: tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
Products: -
?
DRVYIHPFHLLVYS + 3 H2O
DRVY + Ile-His + PFHLL + VYS
-
Substrates: tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
Products: -
?
Gelatin + H2O

?
-
Substrates: -
Products: -
?
Gelatin + H2O
?
-
Substrates: -
Products: -
?
Hemoglobin + H2O

?
-
Substrates: -
Products: -
?
Hemoglobin + H2O
?
-
Substrates: best substrate
Products: -
?
Hemoglobin + H2O
?
-
Substrates: -
Products: -
?
Hemoglobin + H2O
?
-
Substrates: -
Products: -
?
Hemoglobin + H2O
?
-
Substrates: urea-denatured hemoglobin
Products: -
?
Hemoglobin + H2O
?
-
Substrates: urea-denatured hemoglobin
Products: -
?
Hemoglobin + H2O
?
-
Substrates: -
Products: -
?
Myoglobin + H2O

?
-
Substrates: -
Products: -
?
Myoglobin + H2O
?
-
Substrates: -
Products: -
?
proangiotensin + H2O

DRVYIH + PFHLLVYS
-
Substrates: the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
Products: i.e. angiotensin I
?
proangiotensin + H2O
DRVYIH + PFHLLVYS
-
Substrates: the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
Products: i.e. angiotensin I
?
resorufin-labelled casein + H2O

?
Substrates: -
Products: -
?
resorufin-labelled casein + H2O
?
Substrates: -
Products: -
?
soybean isolate protein + H2O

?
Substrates: -
Products: -
?
soybean isolate protein + H2O
?
Substrates: -
Products: -
?
Trypsinogen + H2O

?
-
Substrates: -
Products: -
?
Trypsinogen + H2O
?
-
Substrates: -
Products: -
?
Trypsinogen + H2O
?
-
Substrates: bovine (pancreatic)
Products: -
?
Trypsinogen + H2O
?
-
Substrates: better substrate than chymotrypsinogen
Products: -
?
Trypsinogen + H2O
?
-
Substrates: bovine (trypsinogen)
Products: -
?
Trypsinogen + H2O
?
-
Substrates: bovine (pancreatic)
Products: -
?
Trypsinogen + H2O
?
-
Substrates: bovine (trypsinogen)
Products: -
?
Trypsinogen + H2O
?
-
Substrates: -
Products: -
?
Trypsinogen + H2O
?
-
Substrates: cleaves Lys-Ile and liberates hexapeptide
Products: -
?
Trypsinogen + H2O
?
-
Substrates: cleavage site: Lys6-Ile7
Products: -
?
Trypsinogen + H2O
?
-
Substrates: cleaves Lys-Ile and liberates hexapeptide
Products: -
?
trypsinogen + H2O

trypsin + peptide fragment
-
Substrates: activation by cleavage of a Lys-Pro bond
Products: -
?
trypsinogen + H2O
trypsin + peptide fragment
-
Substrates: activation by cleavage of a Lys-Pro bond
Products: -
?
additional information

?
-
-
Substrates: the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
Products: -
?
additional information
?
-
-
Substrates: the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
Products: -
?
additional information
?
-
-
Substrates: the extracellular enzyme pays a role in development of aspergillosis in lung of mammalia, but it is not essential for virulence
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
?
additional information
?
-
-
Substrates: the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
Products: -
?
additional information
?
-
-
Substrates: specificity
Products: -
?
additional information
?
-
-
Substrates: no hydrolysis of benzyloxycarbonyl-Lys-Gly-Ala, benzyloxycarbonyl-Lys-(D)-Leu-Ala
Products: -
?
additional information
?
-
-
Substrates: the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
?
additional information
?
-
-
Substrates: cleaving ability in decreasing order is hemoglobin, defatted soya flour, gluten, gelatin, skim milk powder
Products: -
-
additional information
?
-
-
Substrates: the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
Products: -
?
additional information
?
-
-
Substrates: specificity
Products: -
?
additional information
?
-
-
Substrates: specificity
Products: -
?
additional information
?
-
-
Substrates: 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'
Products: -
?
additional information
?
-
-
Substrates: no milk clotting activity
Products: -
?
additional information
?
-
-
Substrates: no hydrolysis of benzyloxycarbonyl-Lys-Gly-Ala, benzyloxycarbonyl-Lys-(D)-Leu-Ala
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
?
additional information
?
-
-
Substrates: the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
Products: -
?
additional information
?
-
-
Substrates: no milk clotting activity
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
?
additional information
?
-
Substrates: the propeptide is necessary for catalytic activity
Products: -
?
additional information
?
-
-
Substrates: the propeptide is necessary for catalytic activity
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
?
additional information
?
-
-
Substrates: the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
pepstatin A

-
reversible inhibition
pepstatin A
specific inhibition of the mature enzyme
SDS

-
-
additional information

-
EDTA; diisopropyl phosphofluoridate; no inhibition by p-chloromercuribenzene sulfonate, AgNO3, 2-mercaptoethanol, PMSF
-
additional information
-
diisopropyl phosphofluoridate
-
additional information
-
EDTA; HgCl2, NaF, FeCl3, FeCl2, CoCl2, MgCl2, CaCl2, ZnSO4; PCMB; diisopropyl phosphofluoridate; monoiodoacetate, 1,10-phenanthroline, 6-aminohexanoate
-
additional information
-
Triton X-100; soybean trypsin inhibitor
-
additional information
-
PCMB; diisopropyl phosphofluoridate; monoiodoacetate, 1,10-phenanthroline, 6-aminohexanoate
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 phoenicis, Aspergillus oryzae, 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 phoenicis, Aspergillus niger, 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 phoenicis, Aspergillus niger
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 niger, Aspergillus oryzae, Aspergillus phoenicis, Aspergillus awamori, Aspergillus foetidus, Aspergillus fumigatus, Aspergillus luchuensis, 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 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
Liu, J.; Wang, D.; Wang, H.; Yang, N.; Hou, J.; Lv, X.; Gong, L.
Low frequency magnetic field assisted production of acidic protease by Aspergillus niger
Arch. Microbiol.
206
273
2024
Aspergillus niger
brenda
Lambre, C.; Barat Baviera, J.M.; Bolognesi, C.; Cocconcelli, P.S.; Crebelli, R.; Gott, D.M.; Grob, K.; Lampi, E.; Mengelers, M.; Mortensen, A.; Riviere, G.; Steffensen, I.L.; Tlustos, C.; Van Loveren, H.; Vernis, L.; Zorn, H.; Glandorf, B.; Andryszkiewicz, M.; Gomes, A.; Liu, Y.; Maia, J.; Rainieri, S.; Chesson, A.
Safety evaluation of a food enzyme containing aspergillopepsin I and II from the Aspergillus niger var. macrosporus strain PTG8398
EFSA J.
20
e07471
2022
Aspergillus niger (P55325)
brenda
Purushothaman, K.; Bhat, S.K.; Singh, S.A.; Marathe, G.K.; Appu Rao, A.R.G.
Aspartic protease from Aspergillus niger Molecular characterization and interaction with pepstatin A
Int. J. Biol. Macromol.
139
199-212
2019
Aspergillus niger
brenda
Yoshimura, Y.; Kobayashi, Y.; Kawaguchi, T.; Tani, S.
Improvement of cellulosic biomass-degrading enzyme production by reducing extracellular protease production in Aspergillus aculeatus
J. Gen. Appl. Microbiol.
68
143-150
2022
Aspergillus aculeatus
brenda
Wei, M.; Chen, P.; Zheng, P.; Tao, X.; Yu, X.; Wu, D.
Purification and characterization of aspartic protease from Aspergillus niger and its efficient hydrolysis applications in soy protein degradation
Microb. Cell Fact.
22
42
2023
Aspergillus niger (A2R3L3), Aspergillus niger ATCC MYA-4892 (A2R3L3)
brenda