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Literature summary extracted from
- Secretory expression, purification, characterization, and application of an Aspergillus oryzae prolyl aminopeptidase in Bacillus subtilis (2017), Appl. Biochem. Biotechnol., 181, 1611-1623 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.11.5 | gene pap, recombinant expression of N-terminal His6-tagged enzyme in Bacillus subtilis strain WB600, the enzyme is secreted by adding 2 mM CaCl2 and 5% D-sorbitol, extracellular and intracellular PAP activities are 7.2 and 78.6 U/ml, respectively. Sorbitol and mannitol raise the level of the secretion, but sorbitol is slightly better than mannitol and increases 100.19% compared with the control. CaCl2 can further improve the secretion level of the extracellular enzyme | Aspergillus oryzae |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.11.5 | Cu2+ | strong inhibition | Aspergillus oryzae |  |
| 3.4.11.5 | Zn2+ | strong inhibition | Aspergillus oryzae | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.11.5 | 0.054 | - |
Pro-4-nitroanilide | pH 7.5, 50°C, recombinant enzyme | Aspergillus oryzae | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.11.5 | NaCl | activates at up to over 4 M | Aspergillus oryzae | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.11.5 | Aspergillus oryzae | W8GG09 | - |
- |
| 3.4.11.5 | Aspergillus oryzae JN-412 | W8GG09 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.4.11.5 | recombinant N-terminal His6-tagged PAP 4.3fold from Bacillus subtilis by dialysis, nickel affinity chromatography, and ultrafiltration | Aspergillus oryzae |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.11.5 | additional information | the enzyme cleaves N-terminal Pro residues from many peptides but shows varying hydrolysis rates for various Pro-X dipeptides or peptides of different lengths. The recombinant prolyl aminopeptidase hydrolyzes Pro-4-nitroanilide specifically and no activity is observed toward other 4-nitroanilide substrates. No activity with Leu-Pro. Enzyme PAP can act on casein | Aspergillus oryzae | ? | - |
? | |
| 3.4.11.5 | additional information | the enzyme cleaves N-terminal Pro residues from many peptides but shows varying hydrolysis rates for various Pro-X dipeptides or peptides of different lengths. The recombinant prolyl aminopeptidase hydrolyzes Pro-4-nitroanilide specifically and no activity is observed toward other 4-nitroanilide substrates. No activity with Leu-Pro. Enzyme PAP can act on casein | Aspergillus oryzae JN-412 | ? | - |
? | |
| 3.4.11.5 | Pro-4-nitroanilide + H2O | - |
Aspergillus oryzae | Pro + 4-nitroaniline | - |
? | |
| 3.4.11.5 | Pro-Leu + H2O | 69.5% activity compared to Pro-Phe-Gly-Lys | Aspergillus oryzae | Pro + Leu | - |
? | |
| 3.4.11.5 | Pro-Leu + H2O | 69.5% activity compared to Pro-Phe-Gly-Lys | Aspergillus oryzae JN-412 | Pro + Leu | - |
? | |
| 3.4.11.5 | Pro-Leu-Ser-Arg-Thr-Leu-Ser-Val-Ala-Ala-Lys-Lys + H2O | 17.4% activity compared to Pro-Phe-Gly-Lys | Aspergillus oryzae | Pro + Leu-Ser-Arg-Thr-Leu-Ser-Val-Ala-Ala-Lys-Lys | - |
? | |
| 3.4.11.5 | Pro-Lys + H2O | 74.4% activity compared to Pro-Phe-Gly-Lys | Aspergillus oryzae | Pro + Lys | - |
? | |
| 3.4.11.5 | Pro-Lys + H2O | 74.4% activity compared to Pro-Phe-Gly-Lys | Aspergillus oryzae JN-412 | Pro + Lys | - |
? | |
| 3.4.11.5 | Pro-Phe-Gly-Lys + H2O | best peptide substrate | Aspergillus oryzae | Pro + Phe-Gly-Lys | - |
? | |
| 3.4.11.5 | Pro-Phe-Gly-Lys + H2O | best peptide substrate | Aspergillus oryzae JN-412 | Pro + Phe-Gly-Lys | - |
? | |
| 3.4.11.5 | Pro-Pro + H2O | 44.1% activity compared to Pro-Phe-Gly-Lys | Aspergillus oryzae | Pro + Pro | - |
? | |
| 3.4.11.5 | Pro-Pro + H2O | 44.1% activity compared to Pro-Phe-Gly-Lys | Aspergillus oryzae JN-412 | Pro + Pro | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.11.5 | ? | x * 50000, recombinant His-tagged enzyme, SDS-PAGE | Aspergillus oryzae |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.11.5 | PAP | - |
Aspergillus oryzae |
| 3.4.11.5 | Prolyl aminopeptidase | - |
Aspergillus oryzae |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.5 | 50 | - |
recombinant His-tagged enzyme | Aspergillus oryzae |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.5 | 50 | - |
purified recombinant His-tagged enzyme, stable below | Aspergillus oryzae |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.5 | 7.5 | - |
recombinant His-tagged enzyme | Aspergillus oryzae |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.5 | 6 | 11 | purified recombinant His-tagged enzyme, stable within this range | Aspergillus oryzae |
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