title: Close amino acid sequence relationship between the new plasmid-mediated extended-spectrum beta-lactamase MEN-1 and chromosomally encoded enzymes of Klebsiella oxytoca.
abstract: Isolated from an Escherichia coli strain MEN-1 is a plasmid-mediated beta-lactamase that confers resistance to methoxy imino third-generation cephalosporins. The protein purified to homogeneity was digested by trypsin, chymotrypsin and endoproteinase Asp-N. Amino acid sequence determinations of the resulting peptides gave rise to the alignment of the 263 residues of the beta-lactamase. From amino acid sequence comparison MEN-1 was found to share more than 72% identity with the chromosomally mediated beta-lactamases of Klebsiella oxytoca. Therefore, MEN-1 is the first transferable extended-spectrum beta-lactamase which is not directly derived from the widespread TEMs or SHV-1 penicillinases with which it presents less than 39% identity.
authors.affiliation: Muséum National Histoire Naturelle, CNRS URA 401, Paris, France.
authors.forename: M
authors.initials: M
authors.lastname: Barthélémy
authors.forename: J
authors.initials: J
authors.lastname: Péduzzi
authors.forename: H
authors.initials: H
authors.lastname: Bernard
authors.forename: C
authors.initials: C
authors.lastname: Tancrède
authors.forename: R
authors.initials: R
authors.lastname: Labia
mesh_terms: D000595:Amino Acid Sequence; D002511:Cephalosporins / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D007709:Klebsiella / Q000201:enzymology*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D010957:Plasmids; D016415:Sequence Alignment; D012689:Sequence Homology, Nucleic Acid; D001618:beta-Lactamases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism
chemical_list: D002511:Cephalosporins; D010446:Peptide Fragments; D001618:beta-Lactamases