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Literature summary extracted from
- Truncated prolyl oligopeptidase from Pyrococcus furiosus (2007), Proteins, 69, 633-643.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.21.26 | expression in Escherichia coli | Pyrococcus furiosus |
| 3.4.21.26 | expression of His-tagged full-length and truncated brain enzymes in Escherichia coli strain JM105 | Sus scrofa |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.4.21.26 | additional information | construction of truncated enzyme forms comprising residues 1-72, 1-55, or 1-32 | Pyrococcus furiosus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.21.26 | benzyloxycarbonyl-Pro-prolinal | - |
Pyrococcus furiosus |  |
| 3.4.21.26 | benzyloxycarbonyl-Pro-prolinal | - |
Sus scrofa | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.21.26 | additional information | - |
additional information | kinetics and thermodynamics, and activation parameters, of full-length and truncated enzyme forms | Pyrococcus furiosus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.21.26 | Pyrococcus furiosus | - |
- |
- |
| 3.4.21.26 | Sus scrofa | P23687 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.4.21.26 | recombinant enzyme from Escherichia coli by two different steps of anion exchange chromatography | Pyrococcus furiosus |
Renatured (Commentary)
| EC Number | Renatured (Comment) | Organism |
|---|---|---|
| 3.4.21.26 | after denaturing with urea and guanidinium hydrochloride, the enzyme is refolded by 10fold dilutionin phosphate buffer | Pyrococcus furiosus |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.4.21.26 | brain | - |
Sus scrofa | - |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.26 | additional information | - |
- |
Pyrococcus furiosus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.21.26 | 2-aminobenzoyl-Gly-Phe-Gly-Pro-Phe-Gly-Phe(NO2)-Ala + H2O | - |
Pyrococcus furiosus | ? | - |
? | |
| 3.4.21.26 | azocasein + H2O | - |
Pyrococcus furiosus | ? | - |
? | |
| 3.4.21.26 | benzyloxycarbonyl-Gly-Pro-2-naphthylamide + H2O | - |
Pyrococcus furiosus | benzyloxycarbonyl-Gly-Pro + 2-naphthylamine | - |
? | |
| 3.4.21.26 | benzyloxycarbonyl-Gly-Pro-4-nitroanilide + H2O | - |
Pyrococcus furiosus | benzyloxycarbonyl-Gly-Pro + 4-nitroaniline | - |
? | |
| 3.4.21.26 | benzyloxycarbonyl-Gly-Pro-4-nitrophenyl ester + H2O | - |
Pyrococcus furiosus | benzyloxycarbonyl-Gly-Pro + 4-nitrophenol | - |
? | |
| 3.4.21.26 | benzyloxycarbonyl-Gly-Pro-thiobenzyl ester + H2O | - |
Pyrococcus furiosus | benzyloxycarbonyl-Gly-Pro + phenylmethanethiol | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.21.26 | More | the enzyme consists of two domains, a peptidase and a seven-bladed beta-propeller | Pyrococcus furiosus |
| 3.4.21.26 | More | the enzyme consists of two domains, a peptidase and a seven-bladed beta-propeller, the peptidase domain exhibits an alpha/beta-hydrolase fold contains a central eight-stranded beta-sheet, the beta-propeller of POP is held to the catalytic domain via the two connecting polypeptide main chains, with hydrogen bonds and salt bridges, but mainly with hydrophobic forces | Sus scrofa |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.21.26 | POP | - |
Pyrococcus furiosus |
| 3.4.21.26 | POP | - |
Sus scrofa |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.26 | 55 | - |
assay at, truncated enzyme | Pyrococcus furiosus |
| 3.4.21.26 | 85 | - |
assay at, full-length enzyme | Pyrococcus furiosus |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.26 | 20 | 85 | thermostability of full-length and truncated enzyme forms, overview | Pyrococcus furiosus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.26 | 7 | - |
assay at | Pyrococcus furiosus |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.26 | additional information | - |
pH-dependence of full-length and truncated enzyme forms, overview | Pyrococcus furiosus |
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