JAC Advance Access published online on November 1, 2002
Journal of Antimicrobial Chemotherapy, doi:10.1093/jac/dkf240
© 2002 by The British Society for Antimicrobial Chemotherapy
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In Brief
1 Service de Bactériologie-Virologie,
Hôpital de Bicêtre, Assistance Publique/Hôpitaux
de Paris, Faculté de
Médecine Paris-Sud, 94275 Le Kremlin-Bicêtre,
France
* Corresponding author. E-mail: nordmann.patrice{at}bct.ap-hop-paris.fr.
Received 17 July 2002
; revised 10 September 2002
; accepted 11 September 2002
The extended-spectrum
Keywords: Biochemical analysis of the ceftazidime-hydrolysing
extended-spectrum
-lactamase CTX-M-15
and of its structurally related 
-lactamase
CTX-M-3
2 Sera & Vaccines
Central Research Laboratory,
00725 Warsaw, Poland
-lactamase
CTX-M-15 confers resistance to ceftazidime, unlike the majority
of CTX-M-type enzymes. Kinetic parameters were determined from purified
CTX-M-15 and CTX-M-3, which differ by the single amino acid substitution
Asp-240 to Gly, according to the Ambler numbering of class
A -lactamases. Relative molecular masses
of CTX-M-15 and CTX-M-3 were 
29 kDa
and pI values were 8.9 and 8.4, respectively. CTX-M-15 had higher affinities
for -lactams (lower Km values)
than those of CTX-M-3 but catalytic efficiency (kcat/Km values) was variable depending on
the -lactam substrate. Only CTX-M-15
showed a measurable catalytic efficiency for ceftazidime. Clavulanic
acid and tazobactam were good inhibitors of both enzymes. MICs of -lactams for Escherichia
coli reference strains expressing cloned -lactamase genes
in the same genetic background were similar except for ceftazidime.
This work underlines the fact that some CTX-M enzymes may hydrolyse
ceftazidime and thus confer resistance to this expanded-spectrum
cephalosporin in Enterobacteriaceae.-lactamase, CTX-M,
expanded-spectrum -lactamases
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