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. 2001 Jun;45(6):1868-71.
doi: 10.1128/AAC.45.6.1868-1871.2001.

CENTA as a chromogenic substrate for studying beta-lactamases

C Bebrone  1 , C Moali, F Mahy, S Rival, J D Docquier, G M Rossolini, J Fastrez, R F Pratt, J M Frère, M Galleni
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CENTA as a chromogenic substrate for studying beta-lactamases

C Bebrone et al. Antimicrob Agents Chemother. 2001 Jun.

Abstract

CENTA, a chromogenic cephalosporin, is readily hydrolyzed by beta-lactamases of all classes except for the Aeromonas hydrophila metalloenzyme. Although it cannot practically be used for the detection of beta-lactamase-producing strains on agar plates, it should be quite useful for kinetic studies and the detection of the enzymes in crude extracts and chromatographic fractions.

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Figures

FIG. 1
FIG. 1
Structure of CENTA.
FIG. 2
FIG. 2
Complete hydrolysis of 60 μM CENTA by 20 μM E. cloacae 908R β-lactamase. The light line shows the increase in the A405, and the heavy line shows the decrease in the A260. The ordinate on the right (A260) has been inverted to facilitate the comparison. The optical pathway of the cell was 1 cm.
See this image and copyright information in PMC

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