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Literature summary for 3.4.21.26 extracted from

  • Fülöp, V.; Szeltner, Z.; Renner, V.; Polgar, L.
    Structures of prolyl oligopeptidase substrate/inhibitor complexes. Use of inhibitor binding for titration of the catalytic histidine residue (2001), J. Biol. Chem., 276, 1262-1266.
    View publication on PubMed
Search for more literature for 3.4.21.26

Crystallization (Commentary)

Crystallization (Comment) Organism
S554A mutant enzyme cocrystallized with 2-aminobenzoyl-Gly-Phe-Gly-Pro-Phe-Gly-Phe(NO2)-Ala-NH2 or benzyloxycarbonyl-Gly-Pro-beta-naphthylamide Sus scrofa

Protein Variants

Protein Variants Comment Organism
S554A inactive mutant enzyme Sus scrofa

Inhibitors

Inhibitors Comment Organism Structure
benzyloxycarbonyl-Gly-Pro-beta-naphthylamide
-
 Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa P23687
-
-

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-aminobenzoyl-Gly-Phe-Gly-Pro-Phe-Gly-Phe(NO2)-Ala-NH2 + H2O the enzyme binds no more than six residues, P4-P2' even from a longer substrate Sus scrofa 2-aminobenzoyl-Gly-Phe-Gly-Pro + Phe-Gly-Phe(NO2)-Ala-NH2
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Sus scrofa

pH Range

pH Minimum pH Maximum Comment Organism
6.5 9 about 50% of maximal activity at pH 6.5 and at pH 9.0 Sus scrofa