BETA LACTAMASE I Meaning and
Definition
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Beta lactamase I, also known as penicillinase, refers to a class of enzymes that play a significant role in bacterial resistance to beta-lactam antibiotics. This group of enzymes is capable of hydrolyzing the beta-lactam ring, which is a fundamental structural feature found in numerous antibiotics such as penicillins and cephalosporins. Beta lactamase I is commonly produced by certain pathogenic bacteria including Staphylococcus aureus, Klebsiella pneumoniae, and Escherichia coli.
The hydrolysis of the beta-lactam ring by beta lactamase I results in the inactivation of beta-lactam antibiotics, rendering them ineffective against the bacteria. This enzymatic reaction occurs via nucleophilic attack on the amide bond within the beta-lactam ring, breaking it down into two components. Consequently, this enzymatic activity allows bacteria to resist the bactericidal effects of beta-lactam antibiotics and survive in hostile environments.
The production and presence of beta lactamase I pose a significant challenge in the treatment of bacterial infections. It can lead to treatment failures and necessitate the use of stronger, alternative antibiotics. To combat beta lactamase I-mediated resistance, the development and utilization of beta-lactamase inhibitors, such as clavulanic acid, in combination with beta-lactam antibiotics have been employed. These inhibitors irreversibly bind to beta lactamase I, preventing its enzymatic activity and restoring the efficacy of beta-lactam antibiotics.
Common Misspellings for BETA LACTAMASE I
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