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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
1999-9-3
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pubmed:abstractText |
The DmpA (d-aminopeptidase A) protein produced by Ochrobactrum anthropi hydrolyses p-nitroanilide derivatives of glycine and d-alanine more efficiently than that of l-alanine. When regular peptides are utilized as substrates, the enzyme behaves as an aminopeptidase with a preference for N-terminal residues in an l configuration, thus exemplifying an interesting case of stereospecificity reversal. The best-hydrolysed substrate is l-Ala-Gly-Gly, but tetra- and penta-peptides are also efficiently hydrolysed. The gene encodes a 375-residue precursor, but the active enzyme contains two polypeptides corresponding to residues 2-249 (alpha-subunit) and 250-375 (beta-subunit) of the precursor. Residues 249 and 250 are a Gly and a Ser respectively, and various substitutions performed by site-directed mutagenesis result in the production of an uncleaved and inactive protein. The N-terminal Ser residue of the beta-subunit is followed by a hydrophobic peptide, which is predicted to form a beta-strand structure. All these properties strongly suggest that DmpA is an N-terminal amidohydrolase. An exploration of the databases highlights the presence of a number of open reading frames encoding related proteins in various bacterial genomes. Thus DmpA is very probably the prototype of an original family of N-terminal hydrolases.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10377256-1012018,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10377256-10379365,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/10377256-9280280
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
341 ( Pt 1)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
147-55
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:10377256-Amidohydrolases,
pubmed-meshheading:10377256-Amino Acid Sequence,
pubmed-meshheading:10377256-Aminopeptidases,
pubmed-meshheading:10377256-Bacterial Proteins,
pubmed-meshheading:10377256-Dipeptides,
pubmed-meshheading:10377256-Enzyme Activation,
pubmed-meshheading:10377256-Gram-Negative Bacteria,
pubmed-meshheading:10377256-Molecular Sequence Data,
pubmed-meshheading:10377256-Mutagenesis, Site-Directed,
pubmed-meshheading:10377256-Oligopeptides,
pubmed-meshheading:10377256-Protein Precursors,
pubmed-meshheading:10377256-Recombinant Proteins,
pubmed-meshheading:10377256-Substrate Specificity
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pubmed:year |
1999
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pubmed:articleTitle |
The DmpA aminopeptidase from Ochrobactrum anthropi LMG7991 is the prototype of a new terminal nucleophile hydrolase family.
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pubmed:affiliation |
Laboratoire d'Enzymologie et Centre d'Ingénierie des Protéines, Université de Liège, Institut de Chimie, B6, B-4000 Sart Tilman, Belgium.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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