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Literature summary for 3.4.23.19 extracted from
- Aspergillopepsin II (2004), Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. ), 1, 221-224.
No PubMed abstract available
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| DNA and amino acid sequence determination and analysis, expression in Escherichia coli | Aspergillus niger var. macrosporus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | no inhibition by pepstatin, DAN, and 1.2-epoxy-3-(4-nitrophenoxy)propane | Aspergillus niger var. macrosporus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | the enzyme is secreted | Aspergillus niger var. macrosporus | - |
- |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus niger var. macrosporus | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | the enzyme is synthesized as preproform and performs autoprocessing to the mature enzyme removing the 41-amino acid propeptide and an 11-amino acid intervening peptide, overview | Aspergillus niger var. macrosporus |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native extracellular enzyme from culture medium by ammonium sulfate fractionation, sulfoethyl resin chromatography, and repeated anion exchange chromatography | Aspergillus niger var. macrosporus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| casein + H2O | - |
Aspergillus niger var. macrosporus | ? | - |
? |  |
| Hemoglobin + H2O | substrate from Bos taurus | Aspergillus niger var. macrosporus | ? | - |
? | |
| additional information | the enzyme is a non-pepsin-type acid proteinase, and shows a primary specificity for Tyr, Phe, His, Asn, Asp, Gln, and Glu at P1 position, cleavage site specificity overview | Aspergillus niger var. macrosporus | ? | - |
? | |
| oxidized insulin B chain + H2O | substrate from Bos taurus, cleavage site specificity | Aspergillus niger var. macrosporus | FVN + QHLCGSHLVE + ALYLVCGERGFFY + TPKA | - |
? | |
| oxidized pancreatic ribonuclease A + H2O | substrate from Bos taurus | Aspergillus niger var. macrosporus | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | primary, secondary, and tertiary structure analysis, overview | Aspergillus niger var. macrosporus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Aspergillus proteinase A | - |
Aspergillus niger var. macrosporus |
| More | the enzyme belongs to the A4 peptidase family | Aspergillus niger var. macrosporus |
| Proctase A | - |
Aspergillus niger var. macrosporus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
substrate casein, pH 1.5 | Aspergillus niger var. macrosporus |
| 70 | - |
substrate casein, pH 2.6 | Aspergillus niger var. macrosporus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
the propeptide stabilizes the enzyme against thermal inactivation | Aspergillus niger var. macrosporus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 1.8 | - |
substrate hemoglobin | Aspergillus niger var. macrosporus |
| 2 | - |
substrate casein | Aspergillus niger var. macrosporus |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 6 | - |
stable up to, unstable above with rapid irreversible inactivation | Aspergillus niger var. macrosporus |
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