BRENDA - Reference to 3.4.23.18; Id = 668812

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

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

crystal structure determination and analysis at 2.18 A resolution

Aspergillus phoenicis

additional information

gene disruption leads to 85% reduced extracellular proteolytic activity

Aspergillus niger

pepstatin

-

Aspergillus niger

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

-

34302

-

x * 34302, amino acid sequence calculation

Aspergillus phoenicis

43000

-

x * 43000, SDS-PAGE

Aspergillus niger

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

-

?

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

-

proteolytic modification

the enzyme is synthesized as pro-enzyme

Aspergillus phoenicis

recombinant enzyme from Escherichia coli after solubilization from inclusion bodies by ion exchange chromatography to homogeneity

Aspergillus phoenicis

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

recombinant enzyme from Escherichia coli inclusion bodies by solubilization with 8 M urea and dialysis

Aspergillus phoenicis

commercial preparation

crude enzyme preparation

Aspergillus phoenicis

-

mycelium

-

Aspergillus oryzae

-

mycelium

-

Aspergillus awamori

-

mycelium

-

Aspergillus foetidus

-

mycelium

-

Aspergillus fumigatus

-

mycelium

-

Aspergillus kawachii

-

mycelium

-

Aspergillus niger

-

mycelium

-

Aspergillus phoenicis

-

mycelium

-

Aspergillus sojae

-

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

-

?

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

Acid protease

-

Aspergillus oryzae

Aspartic proteinase

-

Aspergillus oryzae

Aspartic proteinase

-

Aspergillus phoenicis

Aspartic proteinase

-

Aspergillus sojae

aspergillopepsin

-

Aspergillus foetidus

Aspergillopepsin A

-

Aspergillus awamori

Aspergillopepsin A

-

Aspergillus niger

Aspergillopepsin F

-

Aspergillus fumigatus

aspergillopepsin O

-

Aspergillus oryzae

Aspergillopeptidase A

-

Aspergillus phoenicis

Awamorin

-

Aspergillus awamori

carboxyl protease

-

Aspergillus kawachii

carboxyl proteinase I

-

Aspergillus sojae

extracellular aspartic protease

-

Aspergillus fumigatus

extracellular aspartic protease

-

Aspergillus niger

More

the enzyme belongs to the A1 peptidase family

Aspergillus awamori

More

the enzyme belongs to the A1 peptidase family

Aspergillus foetidus

More

the enzyme belongs to the A1 peptidase family

Aspergillus fumigatus

More

the enzyme belongs to the A1 peptidase family

Aspergillus kawachii

More

the enzyme belongs to the A1 peptidase family

Aspergillus niger

More

the enzyme belongs to the A1 peptidase family

Aspergillus oryzae

More

the enzyme belongs to the A1 peptidase family

Aspergillus phoenicis

More

the enzyme belongs to the A1 peptidase family

Aspergillus sojae

PepA

-

Aspergillus niger

PEPO

-

Aspergillus oryzae

Proctase B

-

Aspergillus niger

Proteinase B

-

Aspergillus niger

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

2.2

3

-

Aspergillus sojae

2.5

6

fairly stable

Aspergillus phoenicis

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

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

crystal structure determination and analysis at 2.18 A resolution

Aspergillus phoenicis

additional information

gene disruption leads to 85% reduced extracellular proteolytic activity

Aspergillus niger

pepstatin

-

Aspergillus niger

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

-

34302

-

x * 34302, amino acid sequence calculation

Aspergillus phoenicis

43000

-

x * 43000, SDS-PAGE

Aspergillus niger

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

-

?

proteolytic modification

the enzyme is synthesized as pro-enzyme

Aspergillus phoenicis

recombinant enzyme from Escherichia coli after solubilization from inclusion bodies by ion exchange chromatography to homogeneity

Aspergillus phoenicis

recombinant enzyme from Escherichia coli inclusion bodies by solubilization with 8 M urea and dialysis

Aspergillus phoenicis

commercial preparation

crude enzyme preparation

Aspergillus phoenicis

-

mycelium

-

Aspergillus oryzae

-

mycelium

-

Aspergillus awamori

-

mycelium

-

Aspergillus foetidus

-

mycelium

-

Aspergillus fumigatus

-

mycelium

-

Aspergillus kawachii

-

mycelium

-

Aspergillus niger

-

mycelium

-

Aspergillus phoenicis

-

mycelium

-

Aspergillus sojae

-

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

-

?

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

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

2.2

3

-

Aspergillus sojae

2.5

6

fairly stable

Aspergillus phoenicis

754972

Yoshiya

HAP-01, the first chromogenic ...

Aspergillus oryzae

Org. Biomol. Chem.

17

776-779

2019

-

2

-

2

-

1

-

2

-

753450

Deng

Biocontrol activity of recomb ...

Trichoderma harzianum, Trichoderma harzianum GIM 3.442

Enzyme Microb. Technol.

112

35-42

2018

-

1

-

2

-

6

-

17

-

1

-

2

1

-

1

-

1

-

2

-

6

-

1

-

2

1

-

1

-

1

-

754865

Lim

-

Ginsenoside Rg1 exhibits anti ...

Aspergillus sp.

Nat. Prod. Commun.

13

415-418

2018

-

1

-

2

-

1

-

755227

Liu

The high expression of Asperg ...

Aspergillus pseudoglaucus

Prep. Biochem. Biotechnol.

48

725-733

2018

-

1

-

3

-

1

-

4

1

3

1

-

1

-

2

-

1

-

1

-

4

1

-

1

-

2

-

753407

Yu

-

Construction and application ...

Aspergillus niger

Electron. J. Biotechnol.

29

32-38

2017

-

1

-

1

-

1

-

1

-

754494

Takenaka

Heterologous expression and c ...

Aspergillus pseudoglaucus, Aspergillus pseudoglaucus MK82

J. Sci. Food Agric.

97

95-101

2017

-

1

-

1

4

-

7

-

1

-

4

1

2

1

-

1

-

1

-

1

-

1

-

1

-

4

-

1

-

4

1

-

1

-

1

-

1

-

754932

Yang

Consumption of an acid protea ...

Aspergillus oryzae, Aspergillus oryzae ATCC 42149, Aspergillus oryzae RIB 40

Nutr. Res.

44

60-66

2017

-

8

-

1

-

1

-

1

2

-

1

-

1

-

1

-

1

-

1

-

2

-

752341

Niyonzima

Purification and characteriza ...

Aspergillus terreus, Aspergillus terreus gr.

3 Biotech

5

61-70

2015

4

-

1

17

-

4

-

2

1

-

1

-

1

3

1

-

1

-

1

-

1

-

4

-

1

-

17

-

4

-

1

-

1

-

1

3

1

-

1

-

1

-

753307

Namvar

-

Aspergillus fumigatus proteas ...

Aspergillus fumigatus, Aspergillus fumigatus A1160

Clin. Exp. Allergy

45

982-993

2015

-

2

-

2

-

2

-

2

-

1

-

680281

Landbo

Protease-assisted clarificatio ...

Aspergillus niger

J. Agric. Food Chem.

54

6554-6563

2006

-

1

-

1

-

1

-

1

-

668006

Zhu

Analysis of secreted proteins ...

Aspergillus oryzae, Aspergillus oryzae RIB 40

Biosci. Biotechnol. Biochem.

68

2607-2612

2004

-

1

-

1

-

2

-

5

-

1

-

1

-

2

4

-

1

-

1

-

2

-

1

-

1

-

2

-

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

-

5

1

-

1

-

8

-

2

9

-

10

-

1

9

-

26

6

27

-

4

1

-

5

-

1

-

1

-

8

-

2

9

-

1

9

-

26

6

-

4

1

-

652904

Kamitori

Crystal structures of Aspergil ...

Aspergillus oryzae

J. Mol. Biol.

326

1503-1511

2003

-

1

-

1

-

1

-

2

-

1

-

2

-

1

-

1

-

1

-

1

-

649170

Cho

Structure of aspergillopepsin ...

Aspergillus phoenicis

Acta Crystallogr. Sect. D

57

948-956

2001

-

1

-

2

-

1

-

2

-

1

-

1

-

30556

Lu

Molecular cloning of a cDNA fo ...

Aspergillus awamori, Aspergillus niger, Aspergillus phoenicis

Biosci. Biotechnol. Biochem.

59

954-955

1995

-

3

-

6

-

3

-

5

-

1

-

3

-

3

-

6

-

3

-

1

-

3

-

30558

Tello-Solis

Effect of irreversibility on t ...

Aspergillus phoenicis

Biochem. J.

311

969-974

1995

-

2

-

1

-

1

-

1

-

1

-

30557

Takeuchi

-

Fluorogenic substrate of Asper ...

Aspergillus phoenicis

Agric. Biol. Chem.

52

1279-1280

1988

-

1

-

2

-

1

-

1

-

1

-

3

-

1

-

1

-

1

-

2

-

1

-

1

-

3

-

1

-

1

-

30559

Majima

-

Comparative study on the speci ...

Aspergillus oryzae, Aspergillus phoenicis, Aspergillus sojae

Agric. Biol. Chem.

52

787-793

1988

-

3

-

3

-

3

-

3

-

3

-

30560

Yagi

-

Purification and characterizat ...

Aspergillus kawachii

Agric. Biol. Chem.

50

1029-1033

1986

-

3

-

2

-

2

-

1

-

1

-

2

1

-

1

-

2

-

2

-

2

-

3

-

2

-

2

-

1

-

2

1

-

1

2

-

2

-

2

-

30574

Krishnan

Purification of an acid protea ...

Aspergillus niger

J. Chromatogr.

329

165-170

1985

-

2

-

1

-

1

-

1

-

1

-

30561

Bhumibhamon

-

Precipitation and characterist ...

Aspergillus phoenicis

Thai J. Agric. Sci.

15

157-172

1982

-

2

-

1

-

1

-

1

-

1

-

1

-

2

-

1

-

1

-

1

-

1

-

30562

Panneerselvam

Physico-chemical properties of ...

Aspergillus fumigatus

Ital. J. Biochem.

30

63-74

1981

-

1

-

1

-

1

-

1

-

1

-

1

-

1

-

1

-

1

-

1

-

1

-

1

-

1

-

1

-

1

-

30563

Bhumibhamon

-

Some characreristics of the ac ...

Aspergillus awamori

Thai J. Agric. Sci.

12

27-33

1979

-

1

-

1

-

1

-

1

-

1

-

1

-

1

-

1

-

1

-

30570

Tsujita

Presence and partial character ...

Aspergillus oryzae, Aspergillus oryzae 365-U-64-1

Appl. Environ. Microbiol.

36

237-242

1978

1

-

2

-

3

-

2

-

3

-

1

-

2

1

-

8

-

1

-

2

-

1

-

2

-

3

-

2

-

1

-

2

1

-

8

-

1

-

2

-

30575

Tsujita

Purification and characterizat ...

Aspergillus oryzae

Eur. J. Biochem.

84

347-353

1978

6

-

3

-

2

-

3

-

3

-

1

-

1

2

-

3

-

1

-

2

-

1

-

6

-

3

-

2

-

3

-

1

-

1

2

-

3

-

1

-

2

-

1

-

30571

Tanaka

Purification of an acid protei ...

Aspergillus phoenicis

Biochim. Biophys. Acta

485

406-416

1977

-

1

-

5

-

5

-

30568

Takahashi

The structure and function of ...

Aspergillus niger, Aspergillus phoenicis

J. Biochem.

80

497-506

1976

-

4

-

2

-

2

-

4

-

2

-

30569

Tsujita

Purification and characterizat ...

Aspergillus oryzae

Biochim. Biophys. Acta

445

194-204

1976

-

1

-

3

-

1

3

-

3

-

1

-

1

-

1

5

-

1

-

3

-

1

-

3

-

1

3

-

1

-

1

-

1

5

-

1

-

3

-

30572

Chang

The structure and function of ...

Aspergillus niger

J. Biochem.

80

975-981

1976

-

5

-

5

-

5

-

30573

Iio

Specificity of acid proteinase ...

Aspergillus niger

Biochim. Biophys. Acta

429

912-924

1976

-

2

-

1

-

1

-

1

-

2

-

1

-

1

-

30567

Davidson

Aspergillus oryzae acid protei ...

Aspergillus oryzae

Biochem. J.

147

45-53

1975

-

2

-

2

-

1

-

1

-

6

-

1

-

2

1

-

2

-

2

-

1

-

6

-

1

-

2

1

-

30566

Morihara

Comparative specificity of mic ...

Aspergillus niger, Aspergillus niger B, Aspergillus phoenicis

Arch. Biochem. Biophys.

157

561-572

1973

-

7

-

4

-

22

-

2

-

8

1

-

7

-

22

-

2

-

8

1

-

30565

Kovaleva

The site of diazoacetyl inhibi ...

Aspergillus awamori

Biochem. Biophys. Res. Commun.

49

1075-1081

1972

-

2

-

1

-

1

-

1

-

2

1

-

1

-

2

-

1

-

1

-

2

1

-

30564

Ichishima

-

Purification and mode of assay ...

Aspergillus phoenicis, Aspergillus phoenicis R-3813

Methods Enzymol.

19

397-406

1970

1

-

2

3

1

2

1

3

-

3

-

1

-

3

-

1

6

-

1

-

3

-

2

-

2

-

1

-

2

-

3

-

1

2

1

3

-

1

-

3

-

1

6

-

3

-

2

-

2

-

Aspergillopepsin I

Data extracted from this reference: