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Information on EC 3.4.23.18 - Aspergillopepsin I and Organism(s) Aspergillus oryzae and UniProt Accession Q06902

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     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.23 Aspartic endopeptidases
                3.4.23.18 Aspergillopepsin I
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This record set is specific for:
Aspergillus oryzae
UNIPROT: Q06902 not found.
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The taxonomic range for the selected organisms is: Aspergillus oryzae
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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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
Synonyms
aspartic protease, aspartic proteinase, acid protease, carboxyl proteinase, aspergillopepsin i, carboxyl protease, aspergillopepsin, aspergillopepsin a, aspergillus protease, asp f 13, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid protease
-
Aspergillopepsin A
-
aspergillopepsin O
-
Acid protease
-
-
Aspartic proteinase
-
-
Aspergillopepsin A
-
-
-
-
aspergillopepsin O
-
-
Aspergillus acid protease
-
-
-
-
Aspergillus acid proteinase
-
-
-
-
Aspergillus aspartic proteinase
-
-
-
-
Aspergillus awamori acid proteinase
-
-
-
-
Aspergillus carboxyl proteinase
-
-
-
-
Aspergillus niger acid proteinase
-
-
-
-
Aspergillus saitoi acid proteinase
-
-
-
-
Avamorin
-
-
-
-
Carboxyl proteinase
-
-
-
-
Denapsin
-
-
-
-
Denapsin XP 271
-
-
-
-
Pepsin-type aspartic proteinase
-
-
-
-
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
-
-
-
-
additional information
-
the enzyme belongs to the A1 peptidase family
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9025-49-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
angiotensin + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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-Phe-Phe 3-(4-pyridyl)propyl ester + H2O
Benzyloxycarbonyl-Ala-Ala-Phe + Phe 3-(4-pyridyl)propyl ester
show the reaction diagram
-
-
-
?
Benzyloxycarbonyl-His-Phe-Phe ethyl ester + H2O
Benzyloxycarbonyl-His-Phe + Phe ethyl ester
show the reaction diagram
-
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
?
Chymotrypsinogen + H2O
Pi-Chymotrypsin
show the reaction diagram
Cytochrome c + H2O
?
show the reaction diagram
DRVYIHPFHLLVYS + 3 H2O
DRVY + Ile-His + PFHLL + VYS
show the reaction diagram
-
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
-
-
?
HAP-01 + H2O
?
show the reaction diagram
-
-
-
-
?
Hemoglobin + H2O
?
show the reaction diagram
-
urea-denatured hemoglobin
-
-
?
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
show the reaction diagram
-
-
-
-
ir
Proangiotensin + H2O
?
show the reaction diagram
-
cleavage sites: Tyr-Ile and His-Pro, Aspergillus oryzae enzyme, cleavage specificity compared to pepsin and cathepsin D
-
-
?
Trypsinogen + H2O
?
show the reaction diagram
additional information
?
-
-
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
DRVYIHPFHLLVYS + 3 H2O
DRVY + Ile-His + PFHLL + VYS
show the reaction diagram
-
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no activation by HgCl2, NaF, FeCl3, FeCl2, CoCl2, MgCl2, CaCl2, ZnSO4
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pepstatin A
specific inhibition of the mature enzyme
N-bromosuccinimide
-
not
pepstatin
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cholesterol
-
activation, acetone-washed membrane-bound enzyme
Diglycerides
-
activation, acetone-washed membrane-bound enzyme
-
monoglycerides
-
activation, acetone-washed membrane-bound enzyme
Phospholipids
-
activation, acetone-washed membrane-bound enzyme
Triton X-100
additional information
-
no activation of membrane-bound enzyme by triglycerides or 1,3-dipalmitin
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.18
chymotrypsinogen
-
35°C, pH 3.5
-
0.1
Trypsinogen
-
35°C, pH 3.5
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.14
chymotrypsinogen
-
35°C, pH 3.5
-
11.3
Trypsinogen
-
35°C, pH 3.5
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
242
purified enzyme, pH 3.0, temperature not specified in the publication
143
-
enzyme form M1, in the presence of Triton X-100
867
-
enzyme form M2, in the presence of Triton X-100
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.7
-
assay at
3
-
cytochrome c
3.2
-
cytochrome c
3.2 - 3.6
-
chymotrypsin, 25°C
4.2
-
urea-denatured hemoglobin
4.5
-
urea-denatured hemoglobin
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.3 - 4.3
-
about half-maximal activity at pH 2.3 and 4.3, cytochrome c
3.5 - 6.5
-
about half-maximal activity at pH 3.5 and 6.5, urea-denatured hemoglobin
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
35
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
the enzyme is isolated from an Amano protease preparation from Aspergillus oryzae, enzyme AcP is purified from Biozyme A
Manually annotated by BRENDA team
enzyme synthesis during formation of germ tubes, the pH droops during germination from pH 5.5 to pH 3.5
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
the enzyme is secreted during germination
-
Manually annotated by BRENDA team
-
2 forms: extracellular and cytoplasmic, the cytoplasmic isozymes are immunologically related to extracellular isozyme A2
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41000
x * 42000, proenzyme, SDS-PAGE, x * 41000, mature enzyme, SDS-PAGE
42000
x * 42000, proenzyme, SDS-PAGE, x * 41000, mature enzyme, SDS-PAGE
100000
-
Aspergillus oryzae, enzyme form M2, gel filtration
2000000
-
Aspergillus oryzae, enzyme form M1, gel filtration
230000
-
Aspergillus oryzae, Triton X-100 treated enzyme, gel filtration
32000
-
Aspergillus oryzae, enzyme form A2, sedimentation analysis
33790
-
amino acid sequence
39400
-
Aspergillus oryzae, sedimentation equilibrium meniscus depletion method
42000
-
Aspergillus oryzae, enzyme form F2, gel filtration
60000
-
Aspergillus oryzae, enzyme form F1, gel filtration
63000
-
Aspergillus oryzae, enzyme form A1, sedimetation analysis
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
the secreted enzyme has a pro-sequence, and is processed pH-dependently at below pH 4.6 to the mature enzyme
glycoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Aspergillus oryzae
-
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
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 6
-
stable in this range, complete inactivation below 2 and above 7
30575
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, in 50 mM sodium acetate, pH 5, stable
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the enzyme is purified by 46fold from an Amano protease preparation from Aspergillus oryzae
cytoplasmic enzyme: partial
-
from crude powder preparation
-
several isoforms (cytoplasmic F1 and F2)
-
several isoforms (extracellular A1 and A2)
-
several isoforms (membrane-bound M1 and M2)
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
proctase B, DNA and amino acid sequence determination and analysis, phylogenetic analysis of Aspergillus
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nutrition
-
Aspergillus oryzae and the extracellular protease play important roles in japanese food production, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team