A pepD-like peptidase from the ruminal bacterium, Prevotella albensis

N. D. Walker, N. R. McEwan, R. J. Wallace

Research output: Contribution to journalArticlepeer-review

12 Citations (Scopus)


Peptidases of Prevotella spp. play an important role in the breakdown of protein to ammonia in the rumen. This study describes a peptidase cloned from Prevotella albensis M384. DNA from P. albensis was used to complement a peptidase-deficient strain of Escherichia coli, CM107. A cloned fragment, Pep581, which enabled growth of E. coli CM107, contained an ORF of 1452 bp, encoding a 484 amino acid residue protein with a calculated molecular weight of 53.2 kDa and a theoretical pI of 4.90. Pep581 shared similar sequence identity of 47% with PepD from E coli, and it was also a metallo-aminopeptidase. A putative catalytic metal binding region was identified in Pep581, similar to that found in the related PepT (a tripeptidase) and PepA (an oligopeptidase). Gel filtration indicated Pep581 was a dimer in its native state, similar to PepD of E. coli. PepD is a broad specificity dipeptidase that has been found in several prokaryotes. The enzyme expressed from Pep581 differed from PepD enzymes previously characterised in that it hydrolysed tri- and oligopeptides in addition to dipeptides, cleaving single amino acids from the N terminus. (C) 2005 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.

Original languageEnglish
Pages (from-to)399-404
Number of pages6
JournalFEMS Microbiology Letters
Issue number2
Publication statusPublished - 15 Feb 2005


  • aminopeptidase
  • Prevotella albensis
  • peptidase
  • rumen
  • Escherichia coli
  • rumen bacteria
  • physicochemical parameters
  • enzyme activity
  • ruminicola
  • microorganisms
  • protein
  • hydrolysis
  • metabolism
  • breakdown


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