Bibliographic Details
| Title: |
A pepD-like peptidase from the ruminal bacterium, Prevotella albensis |
| Authors: |
Walker, Nicola D., McEwan, Neil R.1, Wallace, R. John john.wallace@rowett.ac.uk |
| Source: |
FEMS Microbiology Letters. Feb2005, Vol. 243 Issue 2, p399-404. 6p. |
| Subject Terms: |
*PEPTIDASE, *ESCHERICHIA coli, *RUMEN (Ruminants), *OLIGOPEPTIDES |
| Abstract: |
Abstract: 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 1452bp, 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. [Copyright &y& Elsevier] |
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