3.4.23.18: Aspergillopepsin I
This is an abbreviated version!
For detailed information about Aspergillopepsin I, go to the full flat file.
Word Map on EC 3.4.23.18
-
3.4.23.18
-
cathepsins
-
pepstatin
-
proteinases
-
lysosomal
-
hemoglobin
-
renin
-
candida
-
alzheimer
-
plasmodium
-
albicans
-
plasmepsins
-
beta-secretase
-
falciparum
-
zymogen
-
malaria
-
pepsinogen
-
amyloid
-
chymosin
-
subsite
-
carboxypeptidase
-
mucor
-
flap
-
polyproteins
-
procathepsin
-
scissile
-
peptidomimetic
-
pregnancy-associated
-
beta-amyloid
-
cheese
-
milk-clotting
-
gamma-secretase
-
aspartyl
-
d-like
-
antimalarial
-
rhizopus
-
beta-site
-
abeta
-
angiotensinogen
-
leupeptin
-
isostere
-
prosegment
-
nutrition
-
rhizomucor
-
cynara
-
microplus
-
miehei
-
autoprocessing
-
bace-1
-
parasitica
-
hookworm
-
boophilus
- 3.4.23.18
- cathepsins
- pepstatin
- proteinases
- lysosomal
- hemoglobin
- renin
- candida
- alzheimer
- plasmodium
- albicans
-
plasmepsins
- beta-secretase
- falciparum
- zymogen
- malaria
- pepsinogen
-
amyloid
- chymosin
-
subsite
- carboxypeptidase
- mucor
- flap
- polyproteins
-
procathepsin
-
scissile
-
peptidomimetic
-
pregnancy-associated
- beta-amyloid
-
cheese
-
milk-clotting
- gamma-secretase
-
aspartyl
- d-like
-
antimalarial
- rhizopus
-
beta-site
- abeta
- angiotensinogen
- leupeptin
-
isostere
- prosegment
- nutrition
- rhizomucor
- cynara
- microplus
- miehei
-
autoprocessing
- bace-1
- parasitica
- hookworm
- boophilus
Reaction
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, Aspartic proteinase, aspergillopepsin, Aspergillopepsin A, Aspergillopepsin F, aspergillopepsin I, aspergillopepsin O, Aspergillopeptidase A, Aspergillus acid protease, Aspergillus acid proteinase, Aspergillus aspartic proteinase, Aspergillus awamori acid proteinase, Aspergillus carboxyl proteinase, Aspergillus niger acid proteinase, Aspergillus protease, Aspergillus saitoi acid proteinase, Avamorin, Awamorin, carboxyl protease, Carboxyl proteinase, carboxyl proteinase I, Denapsin, denapsin 2P, Denapsin XP 271, EC 3.4.23.6, extracellular aspartic protease, More, PepA, PEPO, Pepsin-type aspartic proteinase, proApp, Proctase, Proctase B, Proctase P, Proteinase B, Proteinase, Aspergillus acid, Proteinase, Aspergillus awamori acid, Proteinase, Aspergillus kawachii aspartic, Proteinase, Aspergillus saitoi acid, Sumizyme AP, Trypsinogen kinase
ECTree
3.4.23.18 Aspergillopepsin IAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.4.23.18 - Aspergillopepsin I
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
angiotensin + H2O
?
-
cleavage site: Tyr-Ile, not His-Pro, Aspergillus oryzae enzyme, cleavage specificity compared to pepsin and cathepsin D
-
-
?
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser + H2O
?
-
i.e. tetradecapeptide of a renin substrate, cleavage sites: Tyr-Ile, His-Pro, Leu-Val, Aspergillus oryzae enzyme, cleavage specificity compared to pepsin and cathepsin D
-
-
?
Benzyloxycarbonyl-Ala-Ala-Lys-Ala-Ala-Ala + H2O
Benzyloxycarbonyl-Ala-Ala-Lys + Ala-Ala-Ala
-
best substrate
-
?
Benzyloxycarbonyl-Ala-Ala-Phe-Phe 3-(4-pyridyl)propyl ester + H2O
Benzyloxycarbonyl-Ala-Ala-Phe + Phe 3-(4-pyridyl)propyl ester
-
-
-
?
Benzyloxycarbonyl-Ala-Lys-Ala-Ala-Ala + H2O
Benzyloxycarbonyl-Ala-Lys + Ala-Ala-Ala
-
-
-
?
Benzyloxycarbonyl-His-Phe-Phe ethyl ester + H2O
Benzyloxycarbonyl-His-Phe + Phe ethyl ester
-
-
-
?
Benzyloxycarbonyl-Lys-Ala-Ala-Ala + H2O
Benzyloxycarbonyl-Lys + Ala-Ala-Ala
-
-
-
?
Benzyloxycarbonyl-Lys-Ala-Ala-Ala-Ala + H2O
Benzyloxycarbonyl-Lys + Ala-Ala-Ala-Ala
-
poor substrate
-
?
Benzyloxycarbonyl-Lys-Leu-Ala-Ala + H2O
Benzyloxycarbonyl-Lys + Leu-Ala-Ala
-
-
-
?
Dnp-Ala-Ala-Phe-Phe-Ala-Arg-NH2 + H2O
Dnp-Ala-Ala-Phe + Phe-Ala-Arg-NH2
-
chromogenic synthetic peptide substrate
-
-
?
DRVYIHPFHLLVYS + 3 H2O
DRVY + Ile-His + PFHLL + Val-Tyr-Ser
-
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
-
-
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + 3 H2O
FVNQHLCGSHLVEAL + Tyr + LVCGERGF + FYTPKA
-
substrate is the oxidized insulin B chain, primarily cleavage at Leu15-Tyr16 and Phe24-Phe25, and minor cleavage of Tyr16-Leu17, overview
-
-
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
FVNQHLCGSH + LVEA + Leu + Tyr + LVCGERGF + FYTPKA
-
substrate is the oxidized insulin B chain, cleavage site specificity, overview
-
-
?
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
-
?
tert-Butoxycarbonyl-Ile-Glu-Gly-Arg 4-methylcoumarin 7-amide + H2O
tert-Butoxycarbonyl-Ile-Glu-Gly + Arg 4-methylcoumarin 7-amide
-
-
-
?
tert-Butoxycarbonyl-Leu-Ser-Thr-Arg 4-methylcoumarin 7-amide + H2O
tert-Butoxycarbonyl-Leu-Ser-Thr + Arg 4-methylcoumarin 7-amide
-
-
-
?
trypsinogen + H2O
trypsin + peptide fragment
-
activation by cleavage of a Lys-Pro bond
-
-
?
Benzyloxycarbonyl-Lys-Ala-Ala + H2O
Benzyloxycarbonyl-Lys + Ala-Ala
-
poor substrate
-
?
Benzyloxycarbonyl-Lys-Ala-Ala + H2O
Benzyloxycarbonyl-Lys + Ala-Ala
-
poor substrate
-
?
Benzyloxycarbonyl-Lys-Leu-Ala + H2O
Benzyloxycarbonyl-Lys + Leu-Ala
-
-
-
?
Benzyloxycarbonyl-Lys-Leu-Ala + H2O
Benzyloxycarbonyl-Lys + Leu-Ala
-
-
-
?
Benzyloxycarbonyl-Lys-Leu-Ala + H2O
Benzyloxycarbonyl-Lys + Leu-Ala
-
-
-
?
Benzyloxycarbonyl-Lys-Phe-Ala + H2O
Benzyloxycarbonyl-Lys + Phe-Ala
-
-
-
?
Benzyloxycarbonyl-Lys-Phe-Ala + H2O
Benzyloxycarbonyl-Lys + Phe-Ala
-
-
-
?
Benzyloxycarbonyl-Lys-Phe-Ala + H2O
Benzyloxycarbonyl-Lys + Phe-Ala
-
-
-
?
Chymotrypsinogen + H2O
Pi-Chymotrypsin
-
cleavage site: Arg15-Ile16
-
?
chymotrypsinogen A + H2O
chymotrypsin + peptide fragment
-
activation
-
-
?
chymotrypsinogen A + H2O
chymotrypsin + peptide fragment
-
activation
-
-
?
DRVYIHPFHLLVYS + 3 H2O
DRVY + Ile-His + PFHLL + VYS
-
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
-
-
?
DRVYIHPFHLLVYS + 3 H2O
DRVY + Ile-His + PFHLL + VYS
-
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
-
-
?
DRVYIHPFHLLVYS + 3 H2O
DRVY + Ile-His + PFHLL + VYS
-
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
-
-
?
DRVYIHPFHLLVYS + 3 H2O
DRVY + Ile-His + PFHLL + VYS
-
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
-
-
?
Trypsinogen + H2O
?
-
cleaves Lys-Ile and liberates hexapeptide
-
-
?
additional information
?
-
-
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
-
-
?
additional information
?
-
-
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
-
-
?
additional information
?
-
-
the extracellular enzyme pays a role in development of aspergillosis in lung of mammalia, but it is not essential for virulence
-
-
?
additional information
?
-
-
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys, at pH 5.5 the enzyme shows also an elastolytic activity with elastin Congo red
-
-
?
additional information
?
-
-
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
-
-
?
additional information
?
-
-
no hydrolysis of benzyloxycarbonyl-Lys-Gly-Ala, benzyloxycarbonyl-Lys-(D)-Leu-Ala
-
-
?
additional information
?
-
-
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
-
-
?
additional information
?
-
-
the immediate turbidity levels obtained after treatments of the black currant juice samples with the Denapsin 2P preparation are in the low end of the range
-
-
?
additional information
?
-
-
no hydrolysis of benzyloxycarbonyl-Lys-Gly-Ala, benzyloxycarbonyl-Lys-(D)-Leu-Ala
-
-
?
additional information
?
-
-
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
-
-
?
additional information
?
-
-
does not require a hydrophobic amino acid in P1, P2 or P3 position, prefers substrates with hydrophobic amino acid in P1', less so in P2'
-
-
?
additional information
?
-
-
no hydrolysis of benzyloxycarbonyl-Lys-Gly-Ala, benzyloxycarbonyl-Lys-(D)-Leu-Ala
-
-
?
additional information
?
-
-
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
-
-
?
additional information
?
-
-
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys, no activity with Z-Glu-Tyr or Z-Tyr-Leu, no milk clotting
-
-
?
additional information
?
-
-
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
-
-
?
additional information
?
-
-
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys, no activity with Z-Glu-Tyr or Z-Tyr-Leu, no milk clotting
-
-
?
additional information
?
-
-
the enzyme 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
-
-
?
