1h2x
From Proteopedia
(New page: 200px<br /> <applet load="1h2x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h2x, resolution 1.49Å" /> '''PROLYL OLIGOPEPTIDA...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1H2X is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/ ]] with GOL as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.26 3.4.21.26]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H2X OCA]]. | + | 1H2X is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/ ]] with GOL as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Prolyl_oligopeptidase Prolyl oligopeptidase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.26 3.4.21.26]]. Structure known Active Site: AS1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H2X OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12202494 12202494] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12202494 12202494] | ||
| + | [[Category: Prolyl oligopeptidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Fulop, V.]] | [[Category: Fulop, V.]] | ||
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[[Category: serine protease]] | [[Category: serine protease]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:24:21 2007'' |
Revision as of 10:19, 30 October 2007
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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
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