Purification and properties of a type-II-like dipeptidyl peptidase from the ruminal peptidolytic bacterium, Prevotella albensis M384

H.-D. Kim, N. D. Walker, N. McKain, R. J. Wallace

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

A dipeptidyl peptidase which hydrolyses the synthetic dipeptidyl peptidase (DPP) substrate, Ala2- p -nitroanilide, was purified 193-fold from the ruminal peptidolytic bacterium, Prevotella albensis M384. The enzyme was a homodimer of molecular mass 91 kDa. Its activity against Ala2- p -nitroanilide had optimal pH and temperature of 7.2 and 40°C respectively. Enzyme activity was inhibited by the serine protease inhibitors, PMSF and dichloroisocoumarin, but not by inhibitors of other categories of proteases. Synthetic substrates for DPP-1 (GlyArg- p -nitroanilide, GlyArg-4-methoxy-naphthylamide), DPP-3 (ArgArg-4-methoxynaphthylamide) and DPP-4 (GlyPro-4-methoxynaphthylamide) or for leucine or alanine aminopeptidase were not hydrolysed, nor were di- or tripeptides. N-Acetyl-Ala2- p -nitroanilide was not hydrolysed. Oligopeptides with Ala, Ile, Ser or Val adjacent to the N-terminal amino acid were all hydrolysed, while peptides with basic or acidic residues in the same position were not. The purified DPP from P. albensis is therefore most similar in its catalytic properties to mammalian DPP-2.
Original languageEnglish
Pages (from-to)307-313
Number of pages7
JournalAnaerobe
Volume7
Issue number6
DOIs
Publication statusPublished - Dec 2001

Fingerprint Dive into the research topics of 'Purification and properties of a type-II-like dipeptidyl peptidase from the ruminal peptidolytic bacterium, Prevotella albensis M384'. Together they form a unique fingerprint.

  • Cite this