Source:http://linkedlifedata.com/resource/pubmed/id/15686841
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2005-2-2
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0378-1097
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
243
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
399-404
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15686841-Amino Acid Sequence,
pubmed-meshheading:15686841-Animals,
pubmed-meshheading:15686841-Base Sequence,
pubmed-meshheading:15686841-Dipeptides,
pubmed-meshheading:15686841-Escherichia coli,
pubmed-meshheading:15686841-Molecular Sequence Data,
pubmed-meshheading:15686841-Oligopeptides,
pubmed-meshheading:15686841-Peptide Hydrolases,
pubmed-meshheading:15686841-Prevotella,
pubmed-meshheading:15686841-Rumen,
pubmed-meshheading:15686841-Sequence Alignment,
pubmed-meshheading:15686841-Substrate Specificity
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pubmed:year |
2005
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pubmed:articleTitle |
A pepD-like peptidase from the ruminal bacterium, Prevotella albensis.
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pubmed:affiliation |
Rowett Research Institute, Bucksburn, Aberdeen AB21 9SB, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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