1o6f
From Proteopedia
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PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, D641A MUTANT WITH BOUND PEPTIDE LIGAND SUC-GLY-PRO
Overview
Prolyl oligopeptidase, a serine peptidase unrelated to trypsin and, subtilisin, is implicated in memory disorders and is an important target, of drug design. The catalytic competence of the Asp(641) residue of the, catalytic triad (Ser(554), Asp(641), His(680)) was studied using the D641N, and D641A variants of the enzyme. Both variants displayed 3 orders of, magnitude reduction in k(cat)/K(m) for, benzyloxycarbonyl-Gly-Pro-2-naphthylamide. Using an octapeptide substrate, the decrease was 6 orders of magnitude, whereas with, Z-Gly-Pro-4-nitrophenyl ester there was virtually no change in, k(cat)/K(m). This indicates that the contribution of Asp(641) is very much, dependent on the substrate-leaving group, which was not the case for the, classic serine peptidase, trypsin. The rate constant ... [(full description)]
About this Structure
1O6F is a [Single protein] structure of sequence from [[1]] with SIN and GOL as [ligands]. Active as [Prolyl oligopeptidase], with EC number [3.4.21.26]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Substrate-dependent competency of the catalytic triad of prolyl oligopeptidase., Szeltner Z, Rea D, Juhasz T, Renner V, Mucsi Z, Orosz G, Fulop V, Polgar L, J Biol Chem. 2002 Nov 22;277(47):44597-605. Epub 2002 Sep 11. PMID:12228249
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