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3.4.21.26: prolyl oligopeptidase

This is an abbreviated version!
For detailed information about prolyl oligopeptidase, go to the full flat file.

Word Map on EC 3.4.21.26

Reaction

Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides =

Synonyms

apPEP, cyproase I, EC 3.4.22.18, endoprolylpeptidase, eryngase, FAP, fibroblast activation protein, FlaP, glutenase, membrane-bound PE, More, mPOP, PE, PEP, PepO2, peptidase, postproline endo-, POP, POP Tb, POP Tc80, POPA, POPB, post proline cleaving enzyme, post prolyl cleaving enzyme, post-proline cleaving endopeptidase, post-proline cleaving enzyme, post-proline cutting enzyme, post-proline endopeptidase, postproline cleaving enzyme, postproline endopeptidase, postproline-cleaving enzyme, PPCE, PREP, PREPL A, proline endopeptidase, proline specific prolyl endopeptidase, proline-specific endopeptidase, proly endopeptidase, prolyl endopeptidase, prolyl endoprotease, prolyl oligopeptidase, prolyl oligopeptidase B, prolylendopeptidase, prost-proline cleaving enzyme, PsE, S28A, S28B, TNA1_POP

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.26 prolyl oligopeptidase

Crystallization

Crystallization on EC 3.4.21.26 - prolyl oligopeptidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
inhibitor (6S)-1-chloro-3-[(4-fluorobenzyl)oxy]-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one is co-crystallized within the catalytic site of a human chimeric POP protein which provides a more detailed understanding of how these inhibitors interact with the key residues within the catalytic pocket
-
enzyme with bound inhibitor
-
enzyme in open conformation
wild type enzyme and mutant S477C, hanging drop vapor diffusion method, using 30% (w/v) PEG 8K and 100 mM Tris-HCl (pH 9.0)
D641A and D641N mutants are cocrystallized in presence of substrate benzyloxycarbonyl-Gly-Pro-4-nitroanilide
enzyme in complex with inhibitor benzyloxycarbonyl-Pro-Prolinal, X-ray diffraction structure determination at high resolution
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
S554A mutant enzyme cocrystallized with 2-aminobenzoyl-Gly-Phe-Gly-Pro-Phe-Gly-Phe(NO2)-Ala-NH2 or benzyloxycarbonyl-Gly-Pro-beta-naphthylamide
wild-type enzyme, mutant enzyme Y473F, mutant enzyme Y473F + benzyloxcarbonyl-Pro-prolinal and mutant enzyme S554A + succinyl-Gly-Pro-OH