Journal of Antimicrobial Chemotherapy, Vol 40, 789-795, Copyright © 1997 by The British Society for Antimicrobial Chemotherapy
S Farzaneh, J Peduzzi, L Sofer, A Reynaud, M Barthelemy and R Labia
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.
ORIGINAL ARTICLES
Characterization and amino acid sequence of the OXY-2 group beta- lactamase of pI 5.7 isolated from aztreonam-resistant Klebsiella oxytoca strain HB60
Laboratoire de Chimie, URA 401, IFR 63 CNRS, Museum National d'Histoire Naturelle, Paris, France.
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