cephalosporinase


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Related to cephalosporinase: penicillinase

cephalosporinase

 [sef″ah-lo-spor´in-ās]
an enzyme that hydrolyzes the CO-NH bond in the lactam ring of cephalosporin, converting it to an inactive product.

β-lac·ta·mase

(lak'tă-mās),
An enzyme produced by many species of bacteria that disrupts the four-membered β-lactam ring of penicillin and cephalosporin groups of antibiotics, destroying their antimicrobial activity. The ability of an organism to produce a β-lactamase may be chromosomal and constitutive or a plasmid-associated acquired property.

cephalosporinase

/ceph·a·lo·spo·rin·ase/ (-spor´in-ās) a β-lactamase preferentially acting on cephalosporins.

cephalosporinase

cephalosporinase

an enzyme that hydrolyzes the −CO−NH− bond in the lactam ring of cephalosporin, converting it to an inactive product.
References in periodicals archive ?
Strain CEC93, exhibiting a phenotypic profile indicative of a high level of cephalosporinase expression, was positive for [bla.
Disk diffusion susceptibility testing with antimicrobial drug-containing disks (Sanofi Diagnostics Pasteur, Marnes-la-Coquette, France) (7) was performed with and without cloxacillin (250 mg/L), which is a [beta]-lactam molecule that inhibits in vitro cephalosporinase activity (5).
AmpC cephalosporinase hyperproduction in Acinetobacter baumannii clinical strains.
Resistance to carbapenems is rare in Enterobacteriaceae and may be mediated by 3 mechanisms: hyperproduction of an AmpC-type cephalosporinase combined with decreased drug permeability through the outer membrane, decreased affinity of penicillin-binding proteins that constitute target proteins for carbapenems, and carbapenem-hydrolyzing [beta]-lactamases (1-3).
The spread of third-generation cephalosporin-resistant isolates harboring plasmid-mediated CMY-2 like cephalosporinase among S.
However, two strains, GS553 and GS554, which produced cephalosporinase and penicillinase, showed a clear expansion of the inhibitory zone only when a disk of cefepime, a better detection agent for ESBLs in the presence of an AmpC [beta]-lactamase (30), was used.
AmpC beta-lactamases are clinically important cephalosporinases, confer resistance to cephalothin, cefazolin, cefoxitin, most penicillins and [beta]-lactamase-[beta]-lactamase inhibitor combinations.
A variety of mechanisms may be involved in conferring resistance in these organisms, including inducible chromosomal cephalosporinases, ESBLs and carbapenemases.
This combination of mechanisms for resistance have been described in group 1 cephalosporinases as well (53).
Ertapenem is stable against hydrolysis by a variety of beta-lactamases, including penicillinases, and cephalosporinases and extended spectrum beta-lactamases.
These enzymes are cephalosporinases capable of hydrolyzing all [beta]-lactams to some extent (1).