Abstract
Two beta-lactamase gene regions were characterized by DNA sequencing in eight clinical isolates of Klebsiella oxytoca. The blaOXY-2a region encoded a beta-lactamase nearly identical to OXY-2 (one amino acid residue substituted) and conferred aztreonam and cefuroxime resistance on the K. oxytoca isolates. Overproduction of OXY-2a was caused by a G-to-A substitution of the fifth nucleotide in the -10 consensus sequence of blaOXY-2a. The blaOXY-1a was identified in a susceptible strain, and the OXY-1a enzyme differed from OXY-1 by two amino acid residues.
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