1h2z: Difference between revisions

Revision as of 06:32, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1h2z.png

Template:STRUCTURE 1h2z

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, S554A MUTANT WITH BOUND PEPTIDE LIGAND SUC-GLY-PROPROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, S554A MUTANT WITH BOUND PEPTIDE LIGAND SUC-GLY-PRO

Template:ABSTRACT PUBMED 12202494

About this StructureAbout this Structure

1H2Z is a Single protein structure. Full crystallographic information is available from OCA.

ReferenceReference

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

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OCA

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 {{STRUCTURE_1h2z|  PDB=1h2z  |  SCENE=  }}
-'''PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, S554A MUTANT WITH BOUND PEPTIDE LIGAND SUC-GLY-PRO'''
+===PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, S554A MUTANT WITH BOUND PEPTIDE LIGAND SUC-GLY-PRO===
-==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 group competed with the productive binding mechanism. Unlike most enzyme reactions, catalysis by the wild-type enzyme exhibited positive activation entropy. In contrast, the activation entropy for the Y473F variant was negative, suggesting that the tyrosine OH group is involved in stabilizing both the transition state and the water shell at the active site. Importantly, Tyr(473) is also implicated in the formation of the enzyme-substrate complex. The nonlinear Arrhenius plot suggested a greater significance of the oxyanion binding site at physiological temperature. The results indicated that Tyr(473) was more needed at high pH, at high temperature, and with charged substrates exhibiting "internally competitive inhibition."
+The line below this paragraph, {{ABSTRACT_PUBMED_12202494}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12202494 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_12202494}}
 ==About this Structure==
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 [[Category: Prolyl oligopeptidase]]
 [[Category: Serine protease]]
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