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Literature summary for 3.4.21.26 extracted from

  • Juhasz, T.; Szeltner, Z.; Polgar, L.
    Truncated prolyl oligopeptidase from Pyrococcus furiosus (2007), Proteins, 69, 633-643.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Pyrococcus furiosus
expression of His-tagged full-length and truncated brain enzymes in Escherichia coli strain JM105 Sus scrofa

Protein Variants

Protein Variants Comment Organism
additional information construction of truncated enzyme forms comprising residues 1-72, 1-55, or 1-32 Pyrococcus furiosus

Inhibitors

Inhibitors Comment Organism Structure
benzyloxycarbonyl-Pro-prolinal
-
Pyrococcus furiosus
benzyloxycarbonyl-Pro-prolinal
-
Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics and thermodynamics, and activation parameters, of full-length and truncated enzyme forms Pyrococcus furiosus

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus
-
-
-
Sus scrofa P23687
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli by two different steps of anion exchange chromatography Pyrococcus furiosus

Renatured (Commentary)

Renatured (Comment) Organism
after denaturing with urea and guanidinium hydrochloride, the enzyme is refolded by 10fold dilutionin phosphate buffer Pyrococcus furiosus

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
Sus scrofa
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Pyrococcus furiosus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-aminobenzoyl-Gly-Phe-Gly-Pro-Phe-Gly-Phe(NO2)-Ala + H2O
-
Pyrococcus furiosus ?
-
?
azocasein + H2O
-
Pyrococcus furiosus ?
-
?
benzyloxycarbonyl-Gly-Pro-2-naphthylamide + H2O
-
Pyrococcus furiosus benzyloxycarbonyl-Gly-Pro + 2-naphthylamine
-
?
benzyloxycarbonyl-Gly-Pro-4-nitroanilide + H2O
-
Pyrococcus furiosus benzyloxycarbonyl-Gly-Pro + 4-nitroaniline
-
?
benzyloxycarbonyl-Gly-Pro-4-nitrophenyl ester + H2O
-
Pyrococcus furiosus benzyloxycarbonyl-Gly-Pro + 4-nitrophenol
-
?
benzyloxycarbonyl-Gly-Pro-thiobenzyl ester + H2O
-
Pyrococcus furiosus benzyloxycarbonyl-Gly-Pro + phenylmethanethiol
-
?

Subunits

Subunits Comment Organism
More the enzyme consists of two domains, a peptidase and a seven-bladed beta-propeller Pyrococcus furiosus
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

Synonyms Comment Organism
POP
-
Pyrococcus furiosus
POP
-
Sus scrofa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
assay at, truncated enzyme Pyrococcus furiosus
85
-
assay at, full-length enzyme Pyrococcus furiosus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
20 85 thermostability of full-length and truncated enzyme forms, overview Pyrococcus furiosus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Pyrococcus furiosus

pH Range

pH Minimum pH Maximum Comment Organism
additional information
-
pH-dependence of full-length and truncated enzyme forms, overview Pyrococcus furiosus