Linked Life Data

1909282

Source:http://linkedlifedata.com/resource/pubmed/id/1909282

Statements in which the resource exists.
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pubmed-article:1909282pubmed:abstractTextThe chromosomally encoded beta-lactamase of Klebsiella oxytoca D483 strain, active against all third-generation cephalosporins but ceftazidime, was purified to homogeneity. The pure protein was digested by trypsin, Staphylococcus aureus V8 protease or proteinase Asp-N. Amino acid sequences of the HPLC-separated proteolytic peptides were determined by manual Edman degradation. Overlapping fragments gave the alignment of the 263 residues of the beta-lactamase which presented 90% homology with the beta-lactamase of the K. oxytoca E23004 strain and about 40% homology with the other enzymes of the structural class A. The cefotaximase activity might result from interaction of a threonine residue at position 140 (position 165 in the numbering of Ambler) with the oxyimino group of the antibiotic.lld:pubmed
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pubmed-article:1909282pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:1909282pubmed:articleTitleCefotaxime-hydrolysing activity of the beta-lactamase of Klebsiella oxytoca D488 could be related to a threonine residue at position 140.lld:pubmed
pubmed-article:1909282pubmed:affiliationMuséum National Histoire Naturelle, CNRS URA 401, Paris, France.lld:pubmed
pubmed-article:1909282pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1909282pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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