beta-lactamase

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Related to Beta-lactamases: Carbapenem

beta-lactamase

[¦bād·ə ′lak·tə‚mās]
(microbiology)
A bacterial enzyme that catalyzes the hydrolysis of the lactam ring in some penicillin antibiotics, rendering them ineffective.
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These confirmatory tests based on the detection of cephamycin hydrolysis or Amp-C inhibition will distinguish Amp-C beta-lactamases from ESBLs and porin mutations.
Predominance of CTX-M-15 extended spectrum beta-lactamases in diverse Escherichia coli and Klebsiella pneumoniae from hospital and community patients in Kuwait.
Epidemiology and outcome of bacteremia caused by extended spectrum beta-lactamase (ESBL)-producing Escherichia coli and Klebsiella spp.
AmpC disk test for detection of plasmid-mediated AmpC beta-lactamases in Enterobacteriaceae lacking chromosomal AmpC beta-lactamases.
They are distinct from extended-spectrum beta-lactamases (ESBLs) by their ability to hydrolyse cephamycins and they are not affected by b-lactamase inhibitors.2 In the Ambler structural classification of b-lactamases, AmpC enzymes belong to class C, while in the functional classification scheme of Bush these are assigned to group 3.3
Beta-lactamases are one of the important resistance mechanisms that bacteria use against beta-lactam antibiotics.
Detection of AmpC beta-lactamases and drug resistance of Enterobacter cloacae.
This result can be explained by better hydrolysis of carbapenem substrates by OXA-40-like and OXA-23-like beta-lactamases and less efficient by OXA-58.
Class A, and D beta-lactamases all share a serine residue in the active site, while class B enzymes require the presence of zinc for activity (and hence are referred to as metallo-beta-lactamases).
The Growing Genetic and Functional Diversity of Extended Spectrum Beta-Lactamases. Biomed Res Int 2018; 2018: 9519718.

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