| pubmed-article:9462429 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9462429 | lifeskim:mentions | umls-concept:C1257890 | lld:lifeskim |
| pubmed-article:9462429 | lifeskim:mentions | umls-concept:C0315260 | lld:lifeskim |
| pubmed-article:9462429 | lifeskim:mentions | umls-concept:C0080194 | lld:lifeskim |
| pubmed-article:9462429 | lifeskim:mentions | umls-concept:C0597979 | lld:lifeskim |
| pubmed-article:9462429 | lifeskim:mentions | umls-concept:C0205409 | lld:lifeskim |
| pubmed-article:9462429 | lifeskim:mentions | umls-concept:C0002518 | lld:lifeskim |
| pubmed-article:9462429 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:9462429 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:9462429 | pubmed:dateCreated | 1998-3-12 | lld:pubmed |
| pubmed-article:9462429 | pubmed:abstractText | Klebsiella oxytoca strain HB60 is highly resistant to cefoperazone and aztreonam (MICs = 128 mg/L). It produces a chromosomally encoded beta-lactamase of pI 5.7 which was highly efficient against penicillins, first-generation cephalosporins and cefoperazone, a non-oxyimino third-generation cephalosporin. Aztreonam and oxyimino broad-spectrum cephalosporins were less good substrates. The beta-lactamase activity was susceptible to inhibition by clavulanic acid (IC50 = 1 microM). The enzyme purified to homogeneity had a specific activity towards benzylpenicillin of 3670 U/mg. The 263 amino acid residues of the protein were sequenced by Edman degradation of proteolytic peptides. The beta-lactamase was shown to belong to the OXY-2 group as it had only one amino acid substitution (Asn for Asp at ABL position 197) compared with the beta-lactamase (pI 5.2) from the aztreonam-susceptible K. oxytoca strain SL911 and two substitutions (Ala223 for Val and Asp255 for Asn) compared with the beta-lactamase (pI 6.4) from the aztreonam-resistant K. oxytoca strain D488. These three OXY-2-group enzymes behave in the same way towards beta-lactam antibiotics. The variability in the resistance of these K. oxytoca strains would thus seem to be due to variation in the level of production of the beta-lactamases rather than to structural alteration of the enzymes. | lld:pubmed |
| pubmed-article:9462429 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9462429 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9462429 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9462429 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9462429 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9462429 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9462429 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9462429 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9462429 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9462429 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:9462429 | pubmed:issn | 0305-7453 | lld:pubmed |
| pubmed-article:9462429 | pubmed:author | pubmed-author:BarthélémyMM | lld:pubmed |
| pubmed-article:9462429 | pubmed:author | pubmed-author:LabiaRR | lld:pubmed |
| pubmed-article:9462429 | pubmed:author | pubmed-author:SofenHH | lld:pubmed |
| pubmed-article:9462429 | pubmed:author | pubmed-author:ReynaudAA | lld:pubmed |
| pubmed-article:9462429 | pubmed:author | pubmed-author:PéduzziJJ | lld:pubmed |
| pubmed-article:9462429 | pubmed:author | pubmed-author:FarzanehSS | lld:pubmed |
| pubmed-article:9462429 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9462429 | pubmed:volume | 40 | lld:pubmed |
| pubmed-article:9462429 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9462429 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9462429 | pubmed:pagination | 789-95 | lld:pubmed |
| pubmed-article:9462429 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:9462429 | pubmed:meshHeading | pubmed-meshheading:9462429-... | lld:pubmed |
| pubmed-article:9462429 | pubmed:meshHeading | pubmed-meshheading:9462429-... | lld:pubmed |
| pubmed-article:9462429 | pubmed:meshHeading | pubmed-meshheading:9462429-... | lld:pubmed |
| pubmed-article:9462429 | pubmed:meshHeading | pubmed-meshheading:9462429-... | lld:pubmed |
| pubmed-article:9462429 | pubmed:meshHeading | pubmed-meshheading:9462429-... | lld:pubmed |
| pubmed-article:9462429 | pubmed:meshHeading | pubmed-meshheading:9462429-... | lld:pubmed |
| pubmed-article:9462429 | pubmed:meshHeading | pubmed-meshheading:9462429-... | lld:pubmed |
| pubmed-article:9462429 | pubmed:meshHeading | pubmed-meshheading:9462429-... | lld:pubmed |
| pubmed-article:9462429 | pubmed:meshHeading | pubmed-meshheading:9462429-... | lld:pubmed |
| pubmed-article:9462429 | pubmed:meshHeading | pubmed-meshheading:9462429-... | lld:pubmed |
| pubmed-article:9462429 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9462429 | pubmed:articleTitle | Characterization and amino acid sequence of the OXY-2 group beta-lactamase of pI 5.7 isolated from aztreonam-resistant Klebsiella oxytoca strain HB60. | lld:pubmed |
| pubmed-article:9462429 | pubmed:affiliation | Laboratoire de Chimie, URA 401, IFR 63 CNRS, Muséum National d'Histoire Naturelle, Paris, France. | lld:pubmed |
| pubmed-article:9462429 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9462429 | pubmed:publicationType | Comparative Study | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9462429 | lld:pubmed |
