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Literature summary extracted from
- Optimized expression of prolyl aminopeptidase in Pichia pastoris and its characteristics after glycosylation (2016), World J. Microbiol. Biotechnol., 32, 176 .
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.11.5 | 2-mercaptoethanol | 11% activation at 10 mM | Aspergillus oryzae |  |
| 3.4.11.5 | DTT | 11% activation at 10 mM | Aspergillus oryzae | |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.11.5 | gene pap, codon optimization and synthesis of the modified gene, optimized expression of N-terminally His-tagged prolyl aminopeptidase in Pichia pastoris strain GS115, subcloning in Escherichia coli strain JM109. The N-terminal His-tag has no effect on PAP expression, whereas a C-terminal His-tag inactivates PAP | Aspergillus oryzae |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.11.5 | Co2+ | 27% inhibition at 1 mM | Aspergillus oryzae | |
| 3.4.11.5 | Cu2+ | 90% inhibition at 1 mM | Aspergillus oryzae | |
| 3.4.11.5 | additional information | no inhibition by EDTA at 0.1-10 mM | Aspergillus oryzae | |
| 3.4.11.5 | Ni2+ | 53% inhibition at 1 mM | Aspergillus oryzae | |
| 3.4.11.5 | Zn2+ | 99% inhibition at 1 mM | Aspergillus oryzae | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.11.5 | additional information | poor effects by 1 mM of Mg2+, Mn2+, Ca2+, and Ba2+ | Aspergillus oryzae | |
| 3.4.11.5 | NaCl | 1.5fold activation at 1.5-3.0 M. Enzyme PAP displays better salt tolerance in the presence of 5.0 M NaCl after incubation at 40°C for 30 min | 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 | - |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 3.4.11.5 | glycoprotein | deglycosylation analysis of affinity purified recombinant protein using Endo H | Aspergillus oryzae |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.4.11.5 | recombinant His-tagged enzyme 4.93fold from culture supernatant and 13.38fold from cell lysate of expressing Pichia pastoris strain GS115 by nickel affinity chromatography | Aspergillus oryzae |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.5 | 143.94 | - |
recombinant His-tagged enzyme purified from Pichia pastoris culture supernatant, pH 7.5, 50°C | Aspergillus oryzae |
| 3.4.11.5 | 166.52 | - |
recombinant His-tagged enzyme purified from Pichia pastoris cell lysate, pH 7.5, 50°C | Aspergillus oryzae |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.11.5 | Pro-4-nitroanilide + H2O | - |
Aspergillus oryzae | Pro + 4-nitroaniline | - |
? | |
| 3.4.11.5 | Pro-4-nitroanilide + H2O | - |
Aspergillus oryzae JN-412 | Pro + 4-nitroaniline | - |
? | |
| 3.4.11.5 | Pro-Leu + H2O | - |
Aspergillus oryzae | Pro + Leu | - |
? | |
| 3.4.11.5 | Pro-Leu + H2O | - |
Aspergillus oryzae JN-412 | Pro + Leu | - |
? | |
| 3.4.11.5 | Pro-Lys + H2O | - |
Aspergillus oryzae | Pro + Lys | - |
? | |
| 3.4.11.5 | Pro-Lys + H2O | - |
Aspergillus oryzae JN-412 | Pro + Lys | - |
? | |
| 3.4.11.5 | Pro-Pro + H2O | - |
Aspergillus oryzae | Pro + Pro | - |
? | |
| 3.4.11.5 | Pro-Pro + H2O | - |
Aspergillus oryzae JN-412 | Pro + Pro | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.11.5 | ? | x * 50406, sequence calculation, 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 | 60 | - |
- |
Aspergillus oryzae |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.5 | 50 | - |
purified recombinant enzyme expressed in Pichia pastoris, half-life is approximately 50 h, 75% activity remains after 24 h, 60% after 48 h, whereas the remaining activity of the PAP expressed in Escherichia coli after 1 h at 50°C is only 10% | Aspergillus oryzae |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.5 | 7.5 | - |
- |
Aspergillus oryzae |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.5 | 5 | 12 | activity range of the recombinant enzyme | Aspergillus oryzae |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.5 | 6 | 10 | purified recombinant enzyme expressed in Pichia pastoris, 50°C, 60% activity remaining after 6 h | Aspergillus oryzae |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.4.11.5 | physiological function | prolyl aminopeptidases are specific exopeptidases, serine peptidases, that catalyze the hydrolysis of the N-terminus proline residue of peptides and proteins. Specialized peptidases are essential to the degradation of proline-rich peptides and proteins, such as collagen and gelatin. Collagens, which contain an extremely high percentage of proline residues (20%), are composed of numerous repeats of a tripeptide, Gly-Pro-X | Aspergillus oryzae |
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Release 2023.1 (January 2023)
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