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Literature summary extracted from

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

Application

EC Number Application Comment Organism
3.4.23.18 nutrition Aspergillus awamori and the extracellular protease play important roles in japanese food production, overview Aspergillus awamori
3.4.23.18 nutrition Aspergillus oryzae and the extracellular protease play important roles in japanese food production, overview Aspergillus oryzae
3.4.23.18 nutrition Aspergillus saitoi and the extracellular protease play important roles in japanese food production, overview Aspergillus phoenicis
3.4.23.18 nutrition Aspergillus sojae and the extracellular protease play important roles in japanese food production, overview Aspergillus sojae
3.4.23.18 nutrition Aspergillus species and the extracellular protease play important roles in japanese food production, overview Aspergillus luchuensis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.23.18 DNA and amino acid sequence determination and analysis, phylogenetic analysis of Aspergillus Aspergillus awamori
3.4.23.18 DNA and amino acid sequence determination and analysis, phylogenetic analysis of Aspergillus Aspergillus fumigatus
3.4.23.18 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
3.4.23.18 gene pepA, located on chromosome 1, DNA and amino acid sequence determination and analysis, genetic organization, phylogenetic analysis of Aspergillus Aspergillus niger
3.4.23.18 proctase B, DNA and amino acid sequence determination and analysis, phylogenetic analysis of Aspergillus Aspergillus oryzae

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.23.18 crystal structure determination and analysis at 2.18 A resolution Aspergillus phoenicis

Protein Variants

EC Number Protein Variants Comment Organism
3.4.23.18 additional information gene disruption leads to 85% reduced extracellular proteolytic activity Aspergillus niger

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.23.18 pepstatin
-
 Aspergillus niger

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.23.18 extracellular the enzyme is secreted Aspergillus niger
-
-
3.4.23.18 extracellular the enzyme is secreted Aspergillus oryzae
-
-
3.4.23.18 extracellular the enzyme is secreted Aspergillus phoenicis
-
-
3.4.23.18 extracellular the enzyme is secreted Aspergillus sojae
-
-
3.4.23.18 extracellular the enzyme is secreted Aspergillus awamori
-
-
3.4.23.18 extracellular the enzyme is secreted Aspergillus luchuensis
-
-
3.4.23.18 extracellular the enzyme is secreted Aspergillus fumigatus
-
-
3.4.23.18 extracellular the enzyme is secreted Aspergillus foetidus
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.23.18 34302
-
 x * 34302, amino acid sequence calculation Aspergillus phoenicis
3.4.23.18 43000
-
 x * 43000, SDS-PAGE Aspergillus niger

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.23.18 chymotrypsinogen A + H2O Aspergillus phoenicis activation chymotrypsin + peptide fragment
-
 ?
3.4.23.18 chymotrypsinogen A + H2O Aspergillus phoenicis R-3813 activation chymotrypsin + peptide fragment
-
 ?
3.4.23.18 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
-
 ?
3.4.23.18 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
-
 ?
3.4.23.18 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
-
 ?
3.4.23.18 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
-
 ?
3.4.23.18 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 ?
-
 ?
3.4.23.18 proangiotensin + H2O Aspergillus phoenicis the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid DRVYIH + PFHLLVYS i.e. angiotensin I ?
3.4.23.18 trypsinogen + H2O Aspergillus phoenicis activation by cleavage of a Lys-Pro bond trypsin + peptide fragment
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.23.18 Aspergillus awamori
-
-
-
3.4.23.18 Aspergillus foetidus
-
-
-
3.4.23.18 Aspergillus fumigatus
-
-
-
3.4.23.18 Aspergillus luchuensis
-
-
-
3.4.23.18 Aspergillus niger
-
 var. awamori, gene pepA, and var. macrosporus
-
3.4.23.18 Aspergillus oryzae
-
 gene pepO
-
3.4.23.18 Aspergillus phoenicis
-
 strain ATCC 14332, formerly Aspergillus saitoi
-
3.4.23.18 Aspergillus phoenicis
-
 gene apnS
-
3.4.23.18 Aspergillus phoenicis R-3813
-
 gene apnS
-
3.4.23.18 Aspergillus sojae
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.23.18 proteolytic modification the enzyme is synthesized as pro-enzyme Aspergillus phoenicis

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.23.18 recombinant enzyme from Escherichia coli after solubilization from inclusion bodies by ion exchange chromatography to homogeneity Aspergillus phoenicis

Reaction

EC Number Reaction Comment Organism Reaction ID
3.4.23.18 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
a

Renatured (Commentary)

EC Number Renatured (Comment) Organism
3.4.23.18 recombinant enzyme from Escherichia coli inclusion bodies by solubilization with 8 M urea and dialysis Aspergillus phoenicis

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.23.18 commercial preparation crude enzyme preparation Aspergillus phoenicis
-
3.4.23.18 mycelium
-
 Aspergillus niger
-
3.4.23.18 mycelium
-
 Aspergillus oryzae
-
3.4.23.18 mycelium
-
 Aspergillus phoenicis
-
3.4.23.18 mycelium
-
 Aspergillus sojae
-
3.4.23.18 mycelium
-
 Aspergillus awamori
-
3.4.23.18 mycelium
-
 Aspergillus luchuensis
-
3.4.23.18 mycelium
-
 Aspergillus fumigatus
-
3.4.23.18 mycelium
-
 Aspergillus foetidus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.23.18 casein + H2O milk casein Aspergillus phoenicis ?
-
 ?
3.4.23.18 casein + H2O milk casein Aspergillus phoenicis R-3813 ?
-
 ?
3.4.23.18 chymotrypsinogen A + H2O activation Aspergillus phoenicis chymotrypsin + peptide fragment
-
 ?
3.4.23.18 chymotrypsinogen A + H2O activation Aspergillus phoenicis R-3813 chymotrypsin + peptide fragment
-
 ?
3.4.23.18 Dnp-Ala-Ala-Phe-Phe-Ala-Arg-NH2 + H2O chromogenic synthetic peptide substrate Aspergillus phoenicis Dnp-Ala-Ala-Phe + Phe-Ala-Arg-NH2
-
 ?
3.4.23.18 DRVYIHPFHLLVYS + 3 H2O tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid Aspergillus oryzae DRVY + Ile-His + PFHLL + VYS
-
 ?
3.4.23.18 DRVYIHPFHLLVYS + 3 H2O tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid Aspergillus phoenicis DRVY + Ile-His + PFHLL + VYS
-
 ?
3.4.23.18 DRVYIHPFHLLVYS + 3 H2O tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid Aspergillus sojae DRVY + Ile-His + PFHLL + VYS
-
 ?
3.4.23.18 DRVYIHPFHLLVYS + 3 H2O tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid Aspergillus phoenicis R-3813 DRVY + Ile-His + PFHLL + VYS
-
 ?
3.4.23.18 DRVYIHPFHLLVYS + 3 H2O tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid Aspergillus phoenicis DRVY + Ile-His + PFHLL + Val-Tyr-Ser
-
 ?
3.4.23.18 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 Aspergillus sojae FVNQHLCGSHLVEAL + Tyr + LVCGERGF + FYTPKA
-
 ?
3.4.23.18 FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O substrate is the oxidized insulin B chain, cleavage site specificity, overview Aspergillus phoenicis FVNQHLCGSH + LVEA + Leu + Tyr + LVCGERGF + FYTPKA
-
 ?
3.4.23.18 additional information the extracellular enzyme pays a role in development of aspergillosis in lung of mammalia, but it is not essential for virulence Aspergillus fumigatus ?
-
 ?
3.4.23.18 additional information the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys Aspergillus niger ?
-
 ?
3.4.23.18 additional information the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys Aspergillus oryzae ?
-
 ?
3.4.23.18 additional information the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys Aspergillus phoenicis ?
-
 ?
3.4.23.18 additional information the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys Aspergillus sojae ?
-
 ?
3.4.23.18 additional information the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys Aspergillus awamori ?
-
 ?
3.4.23.18 additional information the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys Aspergillus luchuensis ?
-
 ?
3.4.23.18 additional information the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys Aspergillus foetidus ?
-
 ?
3.4.23.18 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 Aspergillus fumigatus ?
-
 ?
3.4.23.18 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 Aspergillus phoenicis ?
-
 ?
3.4.23.18 additional information the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys Aspergillus phoenicis R-3813 ?
-
 ?
3.4.23.18 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 Aspergillus phoenicis R-3813 ?
-
 ?
3.4.23.18 proangiotensin + H2O the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid Aspergillus phoenicis DRVYIH + PFHLLVYS i.e. angiotensin I ?
3.4.23.18 trypsinogen + H2O activation by cleavage of a Lys-Pro bond Aspergillus phoenicis trypsin + peptide fragment
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.23.18 ? x * 43000, SDS-PAGE Aspergillus niger
3.4.23.18 ? x * 34302, amino acid sequence calculation Aspergillus phoenicis
3.4.23.18 More secondary and three-dimensional structure determination and comparison Aspergillus phoenicis
3.4.23.18 More secondary structure analysis, three-dimensional structure comparison Aspergillus phoenicis
3.4.23.18 More three-dimensional structure comparison Aspergillus niger
3.4.23.18 More three-dimensional structure comparison Aspergillus oryzae
3.4.23.18 More three-dimensional structure comparison Aspergillus awamori

Synonyms

EC Number Synonyms Comment Organism
3.4.23.18 Acid protease
-
 Aspergillus oryzae
3.4.23.18 Aspartic proteinase
-
 Aspergillus oryzae
3.4.23.18 Aspartic proteinase
-
 Aspergillus phoenicis
3.4.23.18 Aspartic proteinase
-
 Aspergillus sojae
3.4.23.18 aspergillopepsin
-
 Aspergillus foetidus
3.4.23.18 Aspergillopepsin A
-
 Aspergillus niger
3.4.23.18 Aspergillopepsin A
-
 Aspergillus awamori
3.4.23.18 Aspergillopepsin F
-
 Aspergillus fumigatus
3.4.23.18 aspergillopepsin O
-
 Aspergillus oryzae
3.4.23.18 Aspergillopeptidase A
-
 Aspergillus phoenicis
3.4.23.18 Awamorin
-
 Aspergillus awamori
3.4.23.18 carboxyl protease
-
 Aspergillus luchuensis
3.4.23.18 carboxyl proteinase I
-
 Aspergillus sojae
3.4.23.18 extracellular aspartic protease
-
 Aspergillus niger
3.4.23.18 extracellular aspartic protease
-
 Aspergillus fumigatus
3.4.23.18 More the enzyme belongs to the A1 peptidase family Aspergillus niger
3.4.23.18 More the enzyme belongs to the A1 peptidase family Aspergillus oryzae
3.4.23.18 More the enzyme belongs to the A1 peptidase family Aspergillus phoenicis
3.4.23.18 More the enzyme belongs to the A1 peptidase family Aspergillus sojae
3.4.23.18 More the enzyme belongs to the A1 peptidase family Aspergillus awamori
3.4.23.18 More the enzyme belongs to the A1 peptidase family Aspergillus luchuensis
3.4.23.18 More the enzyme belongs to the A1 peptidase family Aspergillus fumigatus
3.4.23.18 More the enzyme belongs to the A1 peptidase family Aspergillus foetidus
3.4.23.18 PepA
-
 Aspergillus niger
3.4.23.18 PEPO
-
 Aspergillus oryzae
3.4.23.18 Proctase B
-
 Aspergillus niger
3.4.23.18 Proteinase B
-
 Aspergillus niger

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.23.18 2.5 3 substrate milk casein Aspergillus phoenicis
3.4.23.18 2.7
-
 assay at Aspergillus oryzae
3.4.23.18 2.7
-
 assay at Aspergillus sojae
3.4.23.18 4 4.5 substrates trypsinogen and chymotrypsinogen Aspergillus phoenicis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.23.18 2.2 3
-
 Aspergillus sojae

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.4.23.18 2.5 6 fairly stable Aspergillus phoenicis