1h2x
From Proteopedia
| Line 23: | Line 23: | ||
[[Category: serine protease]] | [[Category: serine protease]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:26:51 2007'' |
Revision as of 13:22, 30 October 2007
|
PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, Y473F MUTANT
Overview
Prolyl oligopeptidase, a member of a new family of serine peptidases, plays an important role in memory disorders. Earlier x-ray, crystallographic investigations indicated that stabilization of the, tetrahedral transition state of the reaction involved hydrogen bond, formation between the oxyanion of the tetrahedral intermediate and the OH, group of Tyr(473). The contribution of the OH group was tested with the, Y473F variant using various substrates. The charged, succinyl-Gly-Pro-4-nitroanilide was hydrolyzed with a much lower, k(cat)/K(m) compared with the neutral, benzyloxycarbonyl-G1y-Pro-2-naphthylamide, although the binding modes of, the two substrates were similar, as shown by x-ray crystallography. This, suggested that electrostatic interactions between Arg(643) and the, succinyl ... [(full description)]
About this Structure
1H2X is a [Single protein] structure of sequence from [[1]] with GOL as [ligand]. Active as [Prolyl oligopeptidase], with EC number [3.4.21.26]. Structure known Active Site: AS1. Full crystallographic information is available from [OCA].
Reference
Electrostatic effects and binding determinants in the catalysis of prolyl oligopeptidase. Site specific mutagenesis at the oxyanion binding site., Szeltner Z, Rea D, Renner V, Fulop V, Polgar L, J Biol Chem. 2002 Nov 8;277(45):42613-22. Epub 2002 Aug 28. PMID:12202494
Page seeded by OCA on Tue Oct 30 15:26:51 2007
