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

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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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  Data: A pepD-like peptidase from the ruminal bacterium, Prevotella albensis
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  Data: <searchLink fieldCode="AR" term="%22Walker%2C+Nicola+D%2E%22">Walker, Nicola D.</searchLink><br /><searchLink fieldCode="AR" term="%22McEwan%2C+Neil+R%2E%22">McEwan, Neil R.</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Wallace%2C+R%2E+John%22">Wallace, R. John</searchLink><i> john.wallace@rowett.ac.uk</i>
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  Data: <searchLink fieldCode="JN" term="%22FEMS+Microbiology+Letters%22">FEMS Microbiology Letters</searchLink>. Feb2005, Vol. 243 Issue 2, p399-404. 6p.
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  Data: *<searchLink fieldCode="DE" term="%22PEPTIDASE%22">PEPTIDASE</searchLink><br />*<searchLink fieldCode="DE" term="%22ESCHERICHIA+coli%22">ESCHERICHIA coli</searchLink><br />*<searchLink fieldCode="DE" term="%22RUMEN+%28Ruminants%29%22">RUMEN (Ruminants)</searchLink><br />*<searchLink fieldCode="DE" term="%22OLIGOPEPTIDES%22">OLIGOPEPTIDES</searchLink>
– Name: Abstract
  Label: Abstract
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  Data: 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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  Data: <i>Copyright of FEMS Microbiology Letters is the property of Oxford University Press / USA and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1016/j.femsle.2004.12.032
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        Text: English
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        Type: general
      – SubjectFull: ESCHERICHIA coli
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      – SubjectFull: RUMEN (Ruminants)
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              Text: Feb2005
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