1uoq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="1uoq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uoq, resolution 2.1&Aring;" /> '''PROLYL OLIGOPEPTIDAS...)
Line 8: Line 8:
==About this Structure==
==About this Structure==
-
1UOQ is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]] 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=1UOQ OCA]].
+
1UOQ is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]] 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=1UOQ OCA]].
==Reference==
==Reference==
Electrostatic environment at the active site of prolyl oligopeptidase is highly influential during substrate binding., Szeltner Z, Rea D, Renner V, Juliano L, Fulop V, Polgar L, J Biol Chem. 2003 Dec 5;278(49):48786-93. Epub 2003 Sep 25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14514675 14514675]
Electrostatic environment at the active site of prolyl oligopeptidase is highly influential during substrate binding., Szeltner Z, Rea D, Renner V, Juliano L, Fulop V, Polgar L, J Biol Chem. 2003 Dec 5;278(49):48786-93. Epub 2003 Sep 25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14514675 14514675]
 +
[[Category: Prolyl oligopeptidase]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
Line 24: Line 25:
[[Category: serine protease]]
[[Category: serine protease]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 18:29:38 2007''
+
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:51:37 2007''

Revision as of 09:46, 30 October 2007


1uoq, resolution 2.1Å

Drag the structure with the mouse to rotate

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, S554A MUTANT WITH BOUND PEPTIDE LIGAND GLU-PHE-SER-PRO

Overview

The positive electrostatic environment of the active site of prolyl, oligopeptidase was investigated by using substrates with glutamic acid at, positions P2, P3, P4, and P5, respectively. The different substrates gave, various pH rate profiles. The pKa values extracted from the curves are, apparent parameters, presumably affected by the nearby charged residues, and do not reflect the ionization of a simple catalytic histidine as found, in the classic serine peptidases like chymotrypsin and subtilisin. The, temperature dependence of kcat/Km did not produce linear Arrhenius plots, indicating different changes in the individual rate constants with the, increase in temperature. This rendered it possible to calculate these, constants, i.e. the formation (k1) and decomposition (k-1) of the, ... [(full description)]

About this Structure

1UOQ is a [Protein complex] structure of sequences from [Sus scrofa] 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 environment at the active site of prolyl oligopeptidase is highly influential during substrate binding., Szeltner Z, Rea D, Renner V, Juliano L, Fulop V, Polgar L, J Biol Chem. 2003 Dec 5;278(49):48786-93. Epub 2003 Sep 25. PMID:14514675

Page seeded by OCA on Tue Oct 30 11:51:37 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools