BRENDA - Enzyme Database show
show all sequences of 3.4.23.18

Aspergillopepsin I

Ichishima, E.; Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. ) 1, 92-99 (2004)
No PubMed abstract available

Data extracted from this reference:

Application
Application
Commentary
Organism
nutrition
Aspergillus awamori and the extracellular protease play important roles in japanese food production, overview
Aspergillus awamori
nutrition
Aspergillus species and the extracellular protease play important roles in japanese food production, overview
Aspergillus kawachii
nutrition
Aspergillus oryzae and the extracellular protease play important roles in japanese food production, overview
Aspergillus oryzae
nutrition
Aspergillus saitoi and the extracellular protease play important roles in japanese food production, overview
Aspergillus phoenicis
nutrition
Aspergillus sojae and the extracellular protease play important roles in japanese food production, overview
Aspergillus sojae
Cloned(Commentary)
Commentary
Organism
DNA and amino acid sequence determination and analysis, phylogenetic analysis of Aspergillus
Aspergillus awamori
DNA and amino acid sequence determination and analysis, phylogenetic analysis of Aspergillus
Aspergillus fumigatus
gene apnS, DNA and amino acid sequence determination and analysis, phylogenetic analysis of Aspergillus, expression of the proenzyme in Saccharomyces cerevisiae, and in Escherichia coli inclusion bodies, expression of the N-terminal sequence in Escherichia coli
Aspergillus phoenicis
gene pepA, located on chromosome 1, DNA and amino acid sequence determination and analysis, genetic organization, phylogenetic analysis of Aspergillus
Aspergillus niger
proctase B, DNA and amino acid sequence determination and analysis, phylogenetic analysis of Aspergillus
Aspergillus oryzae
Crystallization (Commentary)
Crystallization
Organism
crystal structure determination and analysis at 2.18 A resolution
Aspergillus phoenicis
Engineering
Amino acid exchange
Commentary
Organism
additional information
gene disruption leads to 85% reduced extracellular proteolytic activity
Aspergillus niger
Inhibitors
Inhibitors
Commentary
Organism
Structure
pepstatin
-
Aspergillus niger
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
extracellular
the enzyme is secreted
Aspergillus awamori
-
-
extracellular
the enzyme is secreted
Aspergillus foetidus
-
-
extracellular
the enzyme is secreted
Aspergillus fumigatus
-
-
extracellular
the enzyme is secreted
Aspergillus kawachii
-
-
extracellular
the enzyme is secreted
Aspergillus niger
-
-
extracellular
the enzyme is secreted
Aspergillus oryzae
-
-
extracellular
the enzyme is secreted
Aspergillus phoenicis
-
-
extracellular
the enzyme is secreted
Aspergillus sojae
-
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
34302
-
x * 34302, amino acid sequence calculation
Aspergillus phoenicis
43000
-
x * 43000, SDS-PAGE
Aspergillus niger
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
chymotrypsinogen A + H2O
Aspergillus phoenicis
activation
chymotrypsin + peptide fragment
-
-
?
chymotrypsinogen A + H2O
Aspergillus phoenicis R-3813
activation
chymotrypsin + peptide fragment
-
-
?
DRVYIHPFHLLVYS + 3 H2O
Aspergillus oryzae
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
DRVY + Ile-His + PFHLL + VYS
-
-
?
DRVYIHPFHLLVYS + 3 H2O
Aspergillus sojae
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
DRVY + Ile-His + PFHLL + VYS
-
-
?
DRVYIHPFHLLVYS + 3 H2O
Aspergillus phoenicis
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
DRVY + Ile-His + PFHLL + Val-Tyr-Ser
-
-
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + 3 H2O
Aspergillus sojae
substrate is the oxidized insulin B chain, primarily cleavage at Leu15-Tyr16 and Phe24-Phe25, and minor cleavage of Tyr16-Leu17, overview
FVNQHLCGSHLVEAL + Tyr + LVCGERGF + FYTPKA
-
-
?
additional information
Aspergillus fumigatus
the extracellular enzyme pays a role in development of aspergillosis in lung of mammalia, but it is not essential for virulence
?
-
-
-
proangiotensin + H2O
Aspergillus phoenicis
the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
DRVYIH + PFHLLVYS
i.e. angiotensin I
-
?
trypsinogen + H2O
Aspergillus phoenicis
activation by cleavage of a Lys-Pro bond
trypsin + peptide fragment
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Aspergillus awamori
-
-
-
Aspergillus foetidus
-
-
-
Aspergillus fumigatus
-
-
-
Aspergillus kawachii
-
-
-
Aspergillus niger
-
var. awamori, gene pepA, and var. macrosporus
-
Aspergillus oryzae
-
gene pepO
-
Aspergillus phoenicis
-
gene apnS; strain ATCC 14332, formerly Aspergillus saitoi
-
Aspergillus phoenicis R-3813
-
gene apnS
-
Aspergillus sojae
-
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
proteolytic modification
the enzyme is synthesized as pro-enzyme
Aspergillus phoenicis
Purification (Commentary)
Commentary
Organism
recombinant enzyme from Escherichia coli after solubilization from inclusion bodies by ion exchange chromatography to homogeneity
Aspergillus phoenicis
Reaction
Reaction
Commentary
Organism
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
catalytic residues are Asp32 and Asp214 connected by a complex network of hydrogen bonds, a third catalytic residue is Asp76, which is essential for trypsinogen activation at pH 3.0-4.5, the active site flap plays an important role in recognition of basic P1 residues
Aspergillus phoenicis
Renatured (Commentary)
Commentary
Organism
recombinant enzyme from Escherichia coli inclusion bodies by solubilization with 8 M urea and dialysis
Aspergillus phoenicis
Source Tissue
Source Tissue
Commentary
Organism
Textmining
commercial preparation
crude enzyme preparation
Aspergillus phoenicis
-
mycelium
-
Aspergillus awamori
-
mycelium
-
Aspergillus foetidus
-
mycelium
-
Aspergillus fumigatus
-
mycelium
-
Aspergillus kawachii
-
mycelium
-
Aspergillus niger
-
mycelium
-
Aspergillus oryzae
-
mycelium
-
Aspergillus phoenicis
-
mycelium
-
Aspergillus sojae
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
casein + H2O
milk casein
668812
Aspergillus phoenicis
?
-
-
-
?
casein + H2O
milk casein
668812
Aspergillus phoenicis R-3813
?
-
-
-
?
chymotrypsinogen A + H2O
activation
668812
Aspergillus phoenicis
chymotrypsin + peptide fragment
-
-
-
?
chymotrypsinogen A + H2O
activation
668812
Aspergillus phoenicis R-3813
chymotrypsin + peptide fragment
-
-
-
?
Dnp-Ala-Ala-Phe-Phe-Ala-Arg-NH2 + H2O
chromogenic synthetic peptide substrate
668812
Aspergillus phoenicis
Dnp-Ala-Ala-Phe + Phe-Ala-Arg-NH2
-
-
-
?
DRVYIHPFHLLVYS + 3 H2O
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
668812
Aspergillus oryzae
DRVY + Ile-His + PFHLL + VYS
-
-
-
?
DRVYIHPFHLLVYS + 3 H2O
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
668812
Aspergillus phoenicis
DRVY + Ile-His + PFHLL + VYS
-
-
-
?
DRVYIHPFHLLVYS + 3 H2O
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
668812
Aspergillus sojae
DRVY + Ile-His + PFHLL + VYS
-
-
-
?
DRVYIHPFHLLVYS + 3 H2O
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
668812
Aspergillus phoenicis R-3813
DRVY + Ile-His + PFHLL + VYS
-
-
-
?
DRVYIHPFHLLVYS + 3 H2O
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
668812
Aspergillus phoenicis
DRVY + Ile-His + PFHLL + Val-Tyr-Ser
-
-
-
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + 3 H2O
substrate is the oxidized insulin B chain, primarily cleavage at Leu15-Tyr16 and Phe24-Phe25, and minor cleavage of Tyr16-Leu17, overview
668812
Aspergillus sojae
FVNQHLCGSHLVEAL + Tyr + LVCGERGF + FYTPKA
-
-
-
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
substrate is the oxidized insulin B chain, cleavage site specificity, overview
668812
Aspergillus phoenicis
FVNQHLCGSH + LVEA + Leu + Tyr + LVCGERGF + FYTPKA
-
-
-
?
additional information
the extracellular enzyme pays a role in development of aspergillosis in lung of mammalia, but it is not essential for virulence
668812
Aspergillus fumigatus
?
-
-
-
-
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
668812
Aspergillus niger
?
-
-
-
-
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
668812
Aspergillus oryzae
?
-
-
-
-
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
668812
Aspergillus phoenicis
?
-
-
-
-
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
668812
Aspergillus sojae
?
-
-
-
-
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
668812
Aspergillus awamori
?
-
-
-
-
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
668812
Aspergillus kawachii
?
-
-
-
-
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
668812
Aspergillus foetidus
?
-
-
-
-
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
668812
Aspergillus fumigatus
?
-
-
-
-
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
668812
Aspergillus phoenicis
?
-
-
-
-
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
668812
Aspergillus phoenicis R-3813
?
-
-
-
-
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
668812
Aspergillus phoenicis R-3813
?
-
-
-
-
proangiotensin + H2O
the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
668812
Aspergillus phoenicis
DRVYIH + PFHLLVYS
i.e. angiotensin I
-
-
?
trypsinogen + H2O
activation by cleavage of a Lys-Pro bond
668812
Aspergillus phoenicis
trypsin + peptide fragment
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 43000, SDS-PAGE
Aspergillus niger
?
x * 34302, amino acid sequence calculation
Aspergillus phoenicis
More
three-dimensional structure comparison
Aspergillus awamori
More
three-dimensional structure comparison
Aspergillus niger
More
three-dimensional structure comparison
Aspergillus oryzae
More
secondary and three-dimensional structure determination and comparison; secondary structure analysis, three-dimensional structure comparison
Aspergillus phoenicis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2.5
3
substrate milk casein
Aspergillus phoenicis
2.7
-
assay at
Aspergillus oryzae
2.7
-
assay at
Aspergillus sojae
4
4.5
substrates trypsinogen and chymotrypsinogen
Aspergillus phoenicis
pH Range
pH Minimum
pH Maximum
Commentary
Organism
2.2
3
-
Aspergillus sojae
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
2.5
6
fairly stable
Aspergillus phoenicis
Application (protein specific)
Application
Commentary
Organism
nutrition
Aspergillus awamori and the extracellular protease play important roles in japanese food production, overview
Aspergillus awamori
nutrition
Aspergillus species and the extracellular protease play important roles in japanese food production, overview
Aspergillus kawachii
nutrition
Aspergillus oryzae and the extracellular protease play important roles in japanese food production, overview
Aspergillus oryzae
nutrition
Aspergillus saitoi and the extracellular protease play important roles in japanese food production, overview
Aspergillus phoenicis
nutrition
Aspergillus sojae and the extracellular protease play important roles in japanese food production, overview
Aspergillus sojae
Cloned(Commentary) (protein specific)
Commentary
Organism
DNA and amino acid sequence determination and analysis, phylogenetic analysis of Aspergillus
Aspergillus awamori
DNA and amino acid sequence determination and analysis, phylogenetic analysis of Aspergillus
Aspergillus fumigatus
gene pepA, located on chromosome 1, DNA and amino acid sequence determination and analysis, genetic organization, phylogenetic analysis of Aspergillus
Aspergillus niger
proctase B, DNA and amino acid sequence determination and analysis, phylogenetic analysis of Aspergillus
Aspergillus oryzae
gene apnS, DNA and amino acid sequence determination and analysis, phylogenetic analysis of Aspergillus, expression of the proenzyme in Saccharomyces cerevisiae, and in Escherichia coli inclusion bodies, expression of the N-terminal sequence in Escherichia coli
Aspergillus phoenicis
Crystallization (Commentary) (protein specific)
Crystallization
Organism
crystal structure determination and analysis at 2.18 A resolution
Aspergillus phoenicis
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
gene disruption leads to 85% reduced extracellular proteolytic activity
Aspergillus niger
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
pepstatin
-
Aspergillus niger
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
extracellular
the enzyme is secreted
Aspergillus awamori
-
-
extracellular
the enzyme is secreted
Aspergillus foetidus
-
-
extracellular
the enzyme is secreted
Aspergillus fumigatus
-
-
extracellular
the enzyme is secreted
Aspergillus kawachii
-
-
extracellular
the enzyme is secreted
Aspergillus niger
-
-
extracellular
the enzyme is secreted
Aspergillus oryzae
-
-
extracellular
the enzyme is secreted
Aspergillus phoenicis
-
-
extracellular
the enzyme is secreted
Aspergillus sojae
-
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
34302
-
x * 34302, amino acid sequence calculation
Aspergillus phoenicis
43000
-
x * 43000, SDS-PAGE
Aspergillus niger
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
chymotrypsinogen A + H2O
Aspergillus phoenicis
activation
chymotrypsin + peptide fragment
-
-
?
chymotrypsinogen A + H2O
Aspergillus phoenicis R-3813
activation
chymotrypsin + peptide fragment
-
-
?
DRVYIHPFHLLVYS + 3 H2O
Aspergillus oryzae
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
DRVY + Ile-His + PFHLL + VYS
-
-
?
DRVYIHPFHLLVYS + 3 H2O
Aspergillus sojae
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
DRVY + Ile-His + PFHLL + VYS
-
-
?
DRVYIHPFHLLVYS + 3 H2O
Aspergillus phoenicis
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
DRVY + Ile-His + PFHLL + Val-Tyr-Ser
-
-
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + 3 H2O
Aspergillus sojae
substrate is the oxidized insulin B chain, primarily cleavage at Leu15-Tyr16 and Phe24-Phe25, and minor cleavage of Tyr16-Leu17, overview
FVNQHLCGSHLVEAL + Tyr + LVCGERGF + FYTPKA
-
-
?
additional information
Aspergillus fumigatus
the extracellular enzyme pays a role in development of aspergillosis in lung of mammalia, but it is not essential for virulence
?
-
-
-
proangiotensin + H2O
Aspergillus phoenicis
the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
DRVYIH + PFHLLVYS
i.e. angiotensin I
-
?
trypsinogen + H2O
Aspergillus phoenicis
activation by cleavage of a Lys-Pro bond
trypsin + peptide fragment
-
-
?
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
proteolytic modification
the enzyme is synthesized as pro-enzyme
Aspergillus phoenicis
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme from Escherichia coli after solubilization from inclusion bodies by ion exchange chromatography to homogeneity
Aspergillus phoenicis
Renatured (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme from Escherichia coli inclusion bodies by solubilization with 8 M urea and dialysis
Aspergillus phoenicis
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
commercial preparation
crude enzyme preparation
Aspergillus phoenicis
-
mycelium
-
Aspergillus awamori
-
mycelium
-
Aspergillus foetidus
-
mycelium
-
Aspergillus fumigatus
-
mycelium
-
Aspergillus kawachii
-
mycelium
-
Aspergillus niger
-
mycelium
-
Aspergillus oryzae
-
mycelium
-
Aspergillus phoenicis
-
mycelium
-
Aspergillus sojae
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
casein + H2O
milk casein
668812
Aspergillus phoenicis
?
-
-
-
?
casein + H2O
milk casein
668812
Aspergillus phoenicis R-3813
?
-
-
-
?
chymotrypsinogen A + H2O
activation
668812
Aspergillus phoenicis
chymotrypsin + peptide fragment
-
-
-
?
chymotrypsinogen A + H2O
activation
668812
Aspergillus phoenicis R-3813
chymotrypsin + peptide fragment
-
-
-
?
Dnp-Ala-Ala-Phe-Phe-Ala-Arg-NH2 + H2O
chromogenic synthetic peptide substrate
668812
Aspergillus phoenicis
Dnp-Ala-Ala-Phe + Phe-Ala-Arg-NH2
-
-
-
?
DRVYIHPFHLLVYS + 3 H2O
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
668812
Aspergillus oryzae
DRVY + Ile-His + PFHLL + VYS
-
-
-
?
DRVYIHPFHLLVYS + 3 H2O
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
668812
Aspergillus phoenicis
DRVY + Ile-His + PFHLL + VYS
-
-
-
?
DRVYIHPFHLLVYS + 3 H2O
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
668812
Aspergillus sojae
DRVY + Ile-His + PFHLL + VYS
-
-
-
?
DRVYIHPFHLLVYS + 3 H2O
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
668812
Aspergillus phoenicis R-3813
DRVY + Ile-His + PFHLL + VYS
-
-
-
?
DRVYIHPFHLLVYS + 3 H2O
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
668812
Aspergillus phoenicis
DRVY + Ile-His + PFHLL + Val-Tyr-Ser
-
-
-
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + 3 H2O
substrate is the oxidized insulin B chain, primarily cleavage at Leu15-Tyr16 and Phe24-Phe25, and minor cleavage of Tyr16-Leu17, overview
668812
Aspergillus sojae
FVNQHLCGSHLVEAL + Tyr + LVCGERGF + FYTPKA
-
-
-
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
substrate is the oxidized insulin B chain, cleavage site specificity, overview
668812
Aspergillus phoenicis
FVNQHLCGSH + LVEA + Leu + Tyr + LVCGERGF + FYTPKA
-
-
-
?
additional information
the extracellular enzyme pays a role in development of aspergillosis in lung of mammalia, but it is not essential for virulence
668812
Aspergillus fumigatus
?
-
-
-
-
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
668812
Aspergillus niger
?
-
-
-
-
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
668812
Aspergillus oryzae
?
-
-
-
-
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
668812
Aspergillus phoenicis
?
-
-
-
-
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
668812
Aspergillus sojae
?
-
-
-
-
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
668812
Aspergillus awamori
?
-
-
-
-
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
668812
Aspergillus kawachii
?
-
-
-
-
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
668812
Aspergillus foetidus
?
-
-
-
-
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
668812
Aspergillus fumigatus
?
-
-
-
-
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
668812
Aspergillus phoenicis
?
-
-
-
-
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
668812
Aspergillus phoenicis R-3813
?
-
-
-
-
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
668812
Aspergillus phoenicis R-3813
?
-
-
-
-
proangiotensin + H2O
the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
668812
Aspergillus phoenicis
DRVYIH + PFHLLVYS
i.e. angiotensin I
-
-
?
trypsinogen + H2O
activation by cleavage of a Lys-Pro bond
668812
Aspergillus phoenicis
trypsin + peptide fragment
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 43000, SDS-PAGE
Aspergillus niger
?
x * 34302, amino acid sequence calculation
Aspergillus phoenicis
More
three-dimensional structure comparison
Aspergillus awamori
More
three-dimensional structure comparison
Aspergillus niger
More
three-dimensional structure comparison
Aspergillus oryzae
More
secondary and three-dimensional structure determination and comparison; secondary structure analysis, three-dimensional structure comparison
Aspergillus phoenicis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2.5
3
substrate milk casein
Aspergillus phoenicis
2.7
-
assay at
Aspergillus oryzae
2.7
-
assay at
Aspergillus sojae
4
4.5
substrates trypsinogen and chymotrypsinogen
Aspergillus phoenicis
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
2.2
3
-
Aspergillus sojae
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
2.5
6
fairly stable
Aspergillus phoenicis
Other publictions for EC 3.4.23.18
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
680281
Landbo
Protease-assisted clarificatio ...
Aspergillus niger
J. Agric. Food Chem.
54
6554-6563
2006
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668006
Zhu
Analysis of secreted proteins ...
Aspergillus oryzae, Aspergillus oryzae RIB 40
Biosci. Biotechnol. Biochem.
68
2607-2612
2004
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668812
Ichishima
-
Aspergillopepsin I ...
Aspergillus awamori, Aspergillus foetidus, Aspergillus fumigatus, Aspergillus kawachii, Aspergillus niger, Aspergillus oryzae, Aspergillus phoenicis, Aspergillus phoenicis R-3813, Aspergillus sojae
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
92-99
2004
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5
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652904
Kamitori
Crystal structures of Aspergil ...
Aspergillus oryzae
J. Mol. Biol.
326
1503-1511
2003
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649170
Cho
Structure of aspergillopepsin ...
Aspergillus phoenicis
Acta Crystallogr. Sect. D
57
948-956
2001
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30556
Lu
Molecular cloning of a cDNA fo ...
Aspergillus awamori, Aspergillus niger, Aspergillus phoenicis
Biosci. Biotechnol. Biochem.
59
954-955
1995
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30558
Tello-Solis
Effect of irreversibility on t ...
Aspergillus phoenicis
Biochem. J.
311
969-974
1995
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30557
Takeuchi
-
Fluorogenic substrate of Asper ...
Aspergillus phoenicis
Agric. Biol. Chem.
52
1279-1280
1988
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1
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30559
Majima
-
Comparative study on the speci ...
Aspergillus oryzae, Aspergillus phoenicis, Aspergillus sojae
Agric. Biol. Chem.
52
787-793
1988
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3
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3
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3
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30560
Yagi
Purification and characterizat ...
Aspergillus kawachii
Agric. Biol. Chem.
50
1029-1033
1986
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1
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1
2
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2
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2
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30574
Krishnan
Purification of an acid protea ...
Aspergillus niger
J. Chromatogr.
329
165-170
1985
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30561
Bhumibhamon
-
Precipitation and characterist ...
Aspergillus phoenicis
Thai J. Agric. Sci.
15
157-172
1982
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30562
Panneerselvam
Physico-chemical properties of ...
Aspergillus fumigatus
Ital. J. Biochem.
30
63-74
1981
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30563
Bhumibhamon
-
Some characreristics of the ac ...
Aspergillus awamori
Thai J. Agric. Sci.
12
27-33
1979
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30570
Tsujita
Presence and partial character ...
Aspergillus oryzae, Aspergillus oryzae 365-U-64-1
Appl. Environ. Microbiol.
36
237-242
1978
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30575
Tsujita
Purification and characterizat ...
Aspergillus oryzae
Eur. J. Biochem.
84
347-353
1978
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30571
Tanaka
Purification of an acid protei ...
Aspergillus phoenicis
Biochim. Biophys. Acta
485
406-416
1977
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30568
Takahashi
The structure and function of ...
Aspergillus niger, Aspergillus phoenicis
J. Biochem.
80
497-506
1976
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4
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30569
Tsujita
Purification and characterizat ...
Aspergillus oryzae
Biochim. Biophys. Acta
445
194-204
1976
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30572
Chang
The structure and function of ...
Aspergillus niger
J. Biochem.
80
975-981
1976
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30573
Iio
Specificity of acid proteinase ...
Aspergillus niger
Biochim. Biophys. Acta
429
912-924
1976
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30567
Davidson
Aspergillus oryzae acid protei ...
Aspergillus oryzae
Biochem. J.
147
45-53
1975
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30566
Morihara
Comparative specificity of mic ...
Aspergillus niger, Aspergillus niger B, Aspergillus phoenicis
Arch. Biochem. Biophys.
157
561-572
1973
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7
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30565
Kovaleva
The site of diazoacetyl inhibi ...
Aspergillus awamori
Biochem. Biophys. Res. Commun.
49
1075-1081
1972
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30564
Ichishima
-
Purification and mode of assay ...
Aspergillus phoenicis, Aspergillus phoenicis R-3813
Methods Enzymol.
19
397-406
1970
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