Close amino acid sequence relationship between the new plasmid-mediated extended-spectrum beta-lactamase MEN-1 and chromosomally encoded enzymes of Klebsiella oxytoca.
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.
Barthélémy
M
M
Muséum National Histoire Naturelle, CNRS URA 401, Paris, France.
Péduzzi
J
J
Bernard
H
H
Tancrède
C
C
Labia
R
R
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
D002511:Cephalosporins; D010446:Peptide Fragments; D001618:beta-Lactamases