Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties.
Two chromosome-encoded beta-lactamases have been purified from Citrobacter diversus ULA-27. They exhibited slightly different isoelectric points (6.8 and 6.2) and very similar Mr values (congruent to 29,000). Their specificity spectrum was rather wide, since they hydrolysed some cephalosporins with kcat: values similar to those observed with the best penicillin substrates. Cloxacillin, methicillin and imipenem were hydrolysed very slowly. Hydrolysis of azthreonam could not be detected.
Amicosante
G
G
Università degli Studi dell'Aquila, Dipartimento di Scienze e Tecnologie Biomediche e di Biometria, Italy.
Oratore
A
A
Franceschini
N
N
Maccarrone
M
M
Strom
R
R
Galleni
M
M
Frère
J M
JM
D000596:Amino Acids / Q000032:analysis; D002511:Cephalosporins / Q000378:metabolism; D002846:Chromatography, Affinity; D002876:Chromosomes, Bacterial / Q000201:enzymology; D002954:Citrobacter / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D007526:Isoelectric Point; D007527:Isoenzymes / Q000302:isolation & purification*; D007700:Kinetics; D008970:Molecular Weight; D010406:Penicillins / Q000378:metabolism; D013379:Substrate Specificity; D001618:beta-Lactamases / Q000302:isolation & purification*
D000596:Amino Acids; D002511:Cephalosporins; D007527:Isoenzymes; D010406:Penicillins; D001618:beta-Lactamases