Juhasz_2006_FEBS.Lett_580_3493

Reference

Title : Properties of the prolyl oligopeptidase homologue from Pyrococcus furiosus - Juhasz_2006_FEBS.Lett_580_3493
Author(s) : Juhasz T , Szeltner Z , Polgar L
Ref : FEBS Letters , 580 :3493 , 2006
Abstract :

Prolyl oligopeptidase (POP), the paradigm of a serine peptidase family, hydrolyses peptides, but not proteins. The thermophilic POP from Pyrococcus furiosus (Pfu) appeared to be an exception, since it hydrolysed large proteins. Here we demonstrate that the Pfu POP does not display appreciable activity against azocasein. The autolysis observed earlier was an artefact. We have also found that the pH-rate profile is different from that of the mammalian enzyme and the low pK(a) extracted from the curve represents the ionization of the catalytic histidine. We conclude that some oligopeptidases may be true endopeptidases, cleaving at disordered segments of proteins, but with very low efficacy.

PubMedSearch : Juhasz_2006_FEBS.Lett_580_3493
PubMedID: 16714022

Related information

Citations formats

Juhasz T, Szeltner Z, Polgar L (2006)
Properties of the prolyl oligopeptidase homologue from Pyrococcus furiosus
FEBS Letters 580 :3493

Juhasz T, Szeltner Z, Polgar L (2006)
FEBS Letters 580 :3493