1uoq: Difference between revisions
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[[Category: serine protease]] | [[Category: serine protease]] | ||
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Revision as of 17:02, 30 October 2007
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PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, S554A MUTANT WITH BOUND PEPTIDE LIGAND GLU-PHE-SER-PRO
OverviewOverview
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 StructureAbout 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].
ReferenceReference
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
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