Nature of monocyclic beta-lactam antibiotic Nocardicin A to beta-lactamases

Nocardicin A is the antibiotic which was first found to possess a monocyclic beta-lactam ring. This antibiotic was inactivated by the cleavage of its beta-lactam ring. The direct spectrophotometric assay was applied to measure the rate of enzymatic hydrolysis of Nocardicin A. Nocardicin A was highly stable to both chromosomal and plasmid-mediated beta-lactamases. Of the nine beta-lactam antibiotics including cefoxitin and cefuroxime, Nocardicin A was the most stable to the beta-lactamases tested excluding those from Klebsiella oxytoca and Proteus vulgaris. The latter broad-spectrum beta-lactamases hydrolyzed Nocardicin A rather intensively. Extreme stability of Nocardicin A to beta-lactamases was suggested to be due to the combination of its low affinity to the enzymes and stabilization of its monocyclic beta-lactam ring. Nocardicin A was shown to have inducing ability toward beta-lactamases.