Ligand-induced conformational changes in prolyl oligopeptidase: a kinetic approach

Abstract Most kinetic studies of prolyl oligopeptidase (PREP) were performed with the porcine enzyme using modified peptide substrates. Yet recent biophysical studies used the human homolog. Therefore, the aim of this study was to compare the kinetic behavior of human and porcine PREP, as well as to...

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Veröffentlicht in:	Protein engineering, design and selection design and selection, 2017-03, Vol.30 (3), p.219-226
Hauptverfasser:	Van Elzen, R., Schoenmakers, E., Brandt, I., Van Der Veken, P., Lambeir, A.M.
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Enzyme Stability Humans Hydrogen-Ion Concentration Kinetics Mitochondrial Proteins - chemistry Mitochondrial Proteins - metabolism Protein Domains Recombinant Proteins - chemistry Recombinant Proteins - metabolism Serine Endopeptidases - chemistry Serine Endopeptidases - metabolism Swine
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