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Literature summary for 3.4.23.18 extracted from
- Aspergillopepsin I (2004), Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. ), 1, 92-99.
No PubMed abstract available
Application
| Application | Comment | Organism |
|---|---|---|
| nutrition | Aspergillus awamori and the extracellular protease play important roles in japanese food production, overview | Aspergillus awamori |
| 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 |
| nutrition | Aspergillus species and the extracellular protease play important roles in japanese food production, overview | Aspergillus luchuensis |
Cloned(Commentary)
| Cloned (Comment) | 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 (Comment) | Organism |
|---|---|
| crystal structure determination and analysis at 2.18 A resolution | Aspergillus phoenicis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | gene disruption leads to 85% reduced extracellular proteolytic activity | Aspergillus niger |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| pepstatin | - |
Aspergillus niger |  |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| 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 | - |
- |
| extracellular | the enzyme is secreted | Aspergillus awamori | - |
- |
| extracellular | the enzyme is secreted | Aspergillus luchuensis | - |
- |
| extracellular | the enzyme is secreted | Aspergillus fumigatus | - |
- |
| extracellular | the enzyme is secreted | Aspergillus foetidus | - |
- |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 34302 | - |
x * 34302, amino acid sequence calculation | Aspergillus phoenicis |
| 43000 | - |
x * 43000, SDS-PAGE | Aspergillus niger |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus awamori | - |
- |
- |
| Aspergillus foetidus | - |
- |
- |
| Aspergillus fumigatus | - |
- |
- |
| Aspergillus luchuensis | - |
- |
- |
| Aspergillus niger | - |
var. awamori, gene pepA, and var. macrosporus | - |
| Aspergillus oryzae | - |
gene pepO | - |
| Aspergillus phoenicis | - |
strain ATCC 14332, formerly Aspergillus saitoi | - |
| Aspergillus phoenicis | - |
gene apnS | - |
| Aspergillus phoenicis R-3813 | - |
gene apnS | - |
| Aspergillus sojae | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | the enzyme is synthesized as pro-enzyme | Aspergillus phoenicis |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme from Escherichia coli after solubilization from inclusion bodies by ion exchange chromatography to homogeneity | Aspergillus phoenicis |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| 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)
| Renatured (Comment) | Organism |
|---|---|
| recombinant enzyme from Escherichia coli inclusion bodies by solubilization with 8 M urea and dialysis | Aspergillus phoenicis |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| commercial preparation | crude enzyme preparation | Aspergillus phoenicis | - |
| mycelium | - |
Aspergillus niger | - |
| mycelium | - |
Aspergillus oryzae | - |
| mycelium | - |
Aspergillus phoenicis | - |
| mycelium | - |
Aspergillus sojae | - |
| mycelium | - |
Aspergillus awamori | - |
| mycelium | - |
Aspergillus luchuensis | - |
| mycelium | - |
Aspergillus fumigatus | - |
| mycelium | - |
Aspergillus foetidus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| casein + H2O | milk casein | Aspergillus phoenicis | ? | - |
? | |
| casein + H2O | milk casein | Aspergillus phoenicis R-3813 | ? | - |
? | |
| chymotrypsinogen A + H2O | activation | Aspergillus phoenicis | chymotrypsin + peptide fragment | - |
? | |
| chymotrypsinogen A + H2O | activation | Aspergillus phoenicis R-3813 | chymotrypsin + peptide fragment | - |
? | |
| Dnp-Ala-Ala-Phe-Phe-Ala-Arg-NH2 + H2O | chromogenic synthetic peptide substrate | 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 | 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 | 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 | 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 | 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 | 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 | Aspergillus sojae | FVNQHLCGSHLVEAL + Tyr + LVCGERGF + FYTPKA | - |
? | |
| FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O | substrate is the oxidized insulin B chain, cleavage site specificity, overview | 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 | Aspergillus fumigatus | ? | - |
? | |
| additional information | the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys | Aspergillus niger | ? | - |
? | |
| additional information | the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys | Aspergillus oryzae | ? | - |
? | |
| additional information | the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys | Aspergillus phoenicis | ? | - |
? | |
| additional information | the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys | Aspergillus sojae | ? | - |
? | |
| additional information | the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys | Aspergillus awamori | ? | - |
? | |
| additional information | the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys | Aspergillus luchuensis | ? | - |
? | |
| additional information | the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys | 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 | 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 | Aspergillus phoenicis | ? | - |
? | |
| additional information | the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys | 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 | Aspergillus phoenicis R-3813 | ? | - |
? | |
| proangiotensin + H2O | the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid | Aspergillus phoenicis | DRVYIH + PFHLLVYS | i.e. angiotensin I | ? | |
| trypsinogen + H2O | activation by cleavage of a Lys-Pro bond | Aspergillus phoenicis | trypsin + peptide fragment | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 43000, SDS-PAGE | Aspergillus niger |
| ? | x * 34302, amino acid sequence calculation | Aspergillus phoenicis |
| More | secondary and three-dimensional structure determination and comparison | Aspergillus phoenicis |
| More | secondary structure analysis, three-dimensional structure comparison | Aspergillus phoenicis |
| More | three-dimensional structure comparison | Aspergillus niger |
| More | three-dimensional structure comparison | Aspergillus oryzae |
| More | three-dimensional structure comparison | Aspergillus awamori |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Acid protease | - |
Aspergillus oryzae |
| Aspartic proteinase | - |
Aspergillus oryzae |
| Aspartic proteinase | - |
Aspergillus phoenicis |
| Aspartic proteinase | - |
Aspergillus sojae |
| aspergillopepsin | - |
Aspergillus foetidus |
| Aspergillopepsin A | - |
Aspergillus niger |
| Aspergillopepsin A | - |
Aspergillus awamori |
| Aspergillopepsin F | - |
Aspergillus fumigatus |
| aspergillopepsin O | - |
Aspergillus oryzae |
| Aspergillopeptidase A | - |
Aspergillus phoenicis |
| Awamorin | - |
Aspergillus awamori |
| carboxyl protease | - |
Aspergillus luchuensis |
| carboxyl proteinase I | - |
Aspergillus sojae |
| extracellular aspartic protease | - |
Aspergillus niger |
| extracellular aspartic protease | - |
Aspergillus fumigatus |
| 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 |
| More | the enzyme belongs to the A1 peptidase family | Aspergillus awamori |
| More | the enzyme belongs to the A1 peptidase family | Aspergillus luchuensis |
| More | the enzyme belongs to the A1 peptidase family | Aspergillus fumigatus |
| More | the enzyme belongs to the A1 peptidase family | Aspergillus foetidus |
| PepA | - |
Aspergillus niger |
| PEPO | - |
Aspergillus oryzae |
| Proctase B | - |
Aspergillus niger |
| Proteinase B | - |
Aspergillus niger |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | 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 | Comment | Organism |
|---|---|---|---|
| 2.2 | 3 | - |
Aspergillus sojae |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 2.5 | 6 | fairly stable | Aspergillus phoenicis |
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