| pubmed-article:10377256 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10377256 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
| pubmed-article:10377256 | lifeskim:mentions | umls-concept:C0445819 | lld:lifeskim |
| pubmed-article:10377256 | lifeskim:mentions | umls-concept:C0002570 | lld:lifeskim |
| pubmed-article:10377256 | lifeskim:mentions | umls-concept:C0020289 | lld:lifeskim |
| pubmed-article:10377256 | lifeskim:mentions | umls-concept:C0205088 | lld:lifeskim |
| pubmed-article:10377256 | pubmed:dateCreated | 1999-9-3 | lld:pubmed |
| pubmed-article:10377256 | 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. | lld:pubmed |
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| pubmed-article:10377256 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10377256 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10377256 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10377256 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10377256 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10377256 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:10377256 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:10377256 | pubmed:author | pubmed-author:FrèreJ MJM | lld:pubmed |
| pubmed-article:10377256 | pubmed:author | pubmed-author:Van BeeumenJJ | lld:pubmed |
| pubmed-article:10377256 | pubmed:author | pubmed-author:JorisBB | lld:pubmed |
| pubmed-article:10377256 | pubmed:author | pubmed-author:Van... | lld:pubmed |
| pubmed-article:10377256 | pubmed:author | pubmed-author:GoffinCC | lld:pubmed |
| pubmed-article:10377256 | pubmed:author | pubmed-author:DevreeseBB | lld:pubmed |
| pubmed-article:10377256 | pubmed:author | pubmed-author:FanuelLL | lld:pubmed |
| pubmed-article:10377256 | pubmed:author | pubmed-author:CheggourAA | lld:pubmed |
| pubmed-article:10377256 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10377256 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:10377256 | pubmed:volume | 341 ( Pt 1) | lld:pubmed |
| pubmed-article:10377256 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10377256 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10377256 | pubmed:pagination | 147-55 | lld:pubmed |
| pubmed-article:10377256 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:10377256 | pubmed:meshHeading | pubmed-meshheading:10377256... | lld:pubmed |
| pubmed-article:10377256 | pubmed:meshHeading | pubmed-meshheading:10377256... | lld:pubmed |
| pubmed-article:10377256 | pubmed:meshHeading | pubmed-meshheading:10377256... | lld:pubmed |
| pubmed-article:10377256 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10377256 | pubmed:articleTitle | The DmpA aminopeptidase from Ochrobactrum anthropi LMG7991 is the prototype of a new terminal nucleophile hydrolase family. | lld:pubmed |
| pubmed-article:10377256 | pubmed:affiliation | Laboratoire d'Enzymologie et Centre d'Ingénierie des Protéines, Université de Liège, Institut de Chimie, B6, B-4000 Sart Tilman, Belgium. | lld:pubmed |
| pubmed-article:10377256 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10377256 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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