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Literature summary extracted from

  • Szeltner, Z.; Rea, D.; Renner, V.; Juliano, L.; Fulop, V.; Polgar, L.
    Electrostatic environment at the active site of prolyl oligopeptidase is highly influential during substrate binding (2003), J. Biol. Chem., 278, 48786-48793.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.21.26 peptides 2-aminobenzoyl-Gly-Phe-Arg-Pro-Phe(NO2)-Arg-Ala, 2-aminobenzoyl-Gly-Phe-Glu-Pro-Phe(NO2)-Arg-Ala or 2-aminobenzoyl-Glu-Phe-Ser-Pro-Phe(NO2)-Arg-Ala with prolyl oligopeptidase Sus scrofa

Protein Variants

EC Number Protein Variants Comment Organism
3.4.21.26 R252S specificity rate constant for 2-aminobenzoyl-Gly-Glu-Ser-Pro-Phe(NO2)-Arg-Ala is 39% of the wild-type value, for 2-aminobenzoyl-Glu-Phe-Ser-Pro-Phe(NO2)-Arg-Ala nearly identical to wild-type value, for 2-aminobenzoyl-Glu-Gly-Phe-Ser-Pro-Phe(NO2)-Arg-Ala 52% of wild-type value, for benzyloxycarbonyl-Gly-Pro-beta-naphthylamide 78% of the wild-type value Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.21.26 0.4
-
 2-aminobenzoyl-Gly-Phe-Arg-Pro-Phe(NO2)-Arg-Ala
-
 Sus scrofa
3.4.21.26 1.32
-
 2-aminobenzoyl-Glu-Phe-Ser-Pro-Phe(NO2)-Arg-Ala
-
 Sus scrofa
3.4.21.26 1.54
-
 2-aminobenzoyl-Gly-Phe-Glu-Pro-Phe(NO2)-Arg-Ala
-
 Sus scrofa
3.4.21.26 3.7
-
 2-aminobenzoyl-Glu-Gly-Phe-Ser-Pro-Phe(NO2)-Arg-Ala
-
 Sus scrofa
3.4.21.26 6.3
-
 2-aminobenzoyl-Gly-Glu-Ser-Pro-Phe(NO2)-Arg-Ala
-
 Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.26 Sus scrofa P23687
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.21.26 brain
-
 Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.26 2-aminobenzoyl-Glu-Gly-Phe-Ser-Pro-Phe(NO2)-Arg-Ala + H2O
-
 Sus scrofa 2-aminobenzoyl-Glu-Gly-Phe-Ser-Pro + Phe(NO2)-Arg-Ala
-
 ?
3.4.21.26 2-aminobenzoyl-Glu-Phe-Ser-Pro-Phe(NO2)-Arg-Ala + H2O
-
 Sus scrofa 2-aminobenzoyl-Glu-Phe-Ser-Pro + Phe(NO2)-Arg-Ala
-
 ?
3.4.21.26 2-aminobenzoyl-Gly-Glu-Ser-Pro-Phe(NO2)-Arg-Ala + H2O
-
 Sus scrofa 2-aminobenzoyl-Gly-Glu-Ser-Pro + Phe(NO2)-Arg-Ala
-
 ?
3.4.21.26 2-aminobenzoyl-Gly-Phe-Arg-Pro-Phe(NO2)-Arg-Ala + H2O
-
 Sus scrofa 2-aminobenzoyl-Gly-Phe-Arg-Pro + Phe(NO2)-Arg-Ala
-
 ?
3.4.21.26 2-aminobenzoyl-Gly-Phe-Glu-Pro-Phe(NO2)-Arg-Ala + H2O
-
 Sus scrofa 2-aminobenzoyl-Gly-Phe-Glu-Pro + Phe(NO2)-Arg-Ala
-
 ?
3.4.21.26 benzyloxycarbonyl-Gly-Pro-beta-naphthylamide + H2O
-
 Sus scrofa benzyloxycarbonyl-Gly-Pro + beta-naphthylamine
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.21.26 0.03 0.55 2-aminobenzoyl-Glu-Gly-Phe-Ser-Pro-Phe(NO2)-Arg-Ala
-
 Sus scrofa
3.4.21.26 1.7
-
 2-aminobenzoyl-Glu-Phe-Ser-Pro-Phe(NO2)-Arg-Ala
-
 Sus scrofa
3.4.21.26 1.82
-
 2-aminobenzoyl-Gly-Glu-Ser-Pro-Phe(NO2)-Arg-Ala
-
 Sus scrofa
3.4.21.26 2.4
-
 2-aminobenzoyl-Gly-Phe-Glu-Pro-Phe(NO2)-Arg-Ala
-
 Sus scrofa
3.4.21.26 2.94
-
 2-aminobenzoyl-Gly-Glu-Ser-Pro-Phe(NO2)-Arg-Ala
-
 Sus scrofa
3.4.21.26 3.2
-
 2-aminobenzoyl-Gly-Phe-Arg-Pro-Phe(NO2)-Arg-Ala
-
 Sus scrofa
3.4.21.26 7.22
-
 2-aminobenzoyl-Glu-Gly-Phe-Ser-Pro-Phe(NO2)-Arg-Ala
-
 Sus scrofa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.21.26 6.6
-
 2-aminobenzoyl-Glu-Gly-Phe-Ser-Pro-Phe(NO2)-Arg-Ala Sus scrofa
3.4.21.26 7
-
 2-aminobenzoyl-Gly-Glu-Ser-Pro-Phe(NO2)-Arg-Ala Sus scrofa
3.4.21.26 7.9
-
 2-aminobenzoyl-Glu-Phe-Ser-Pro-Phe(NO2)-Arg-Ala Sus scrofa
3.4.21.26 7.9
-
 2-aminobenzoyl-Gly-Phe-Glu-Pro-Phe(NO2)-Arg-Ala Sus scrofa
3.4.21.26 8.5
-
 above, 2-aminobenzoyl-Gly-Phe-Arg-Pro-Phe(NO2)-Arg-Ala Sus scrofa

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.21.26 additional information
-
-
 Sus scrofa