CENTA as a chromogenic substrate for studying beta-lactamases.
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.
Bebrone
C
C
Centre for Protein Engineering, University of Liège, Institut de Chimie B6, Sart Tilman, 4000 Liège, Belgium.
Moali
C
C
Mahy
F
F
Rival
S
S
Docquier
J D
JD
Rossolini
G M
GM
Fastrez
J
J
Pratt
R F
RF
Frère
J M
JM
Galleni
M
M
D002511:Cephalosporins; D002863:Chromogenic Compounds; D007202:Indicators and Reagents; D007700:Kinetics; D009169:Mycobacterium tuberculosis / Q000201:enzymology; D011550:Pseudomonas aeruginosa / Q000201:enzymology; D013211:Staphylococcus aureus / Q000201:enzymology; D001618:beta-Lactamases / Q000378:metabolism*
D002511:Cephalosporins; D002863:Chromogenic Compounds; D007202:Indicators and Reagents; C034025:CENTA; D001618:beta-Lactamases; C021720:nitrocefin