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.
Kojo
H
H
Research Laboratories, Fujisawa Pharmaceutical Co., Ltd., Ibaraki.
Mine
Y
Y
Nishida
M
M
Goto
S
S
Kuwahara
S
S
D000900:Anti-Bacterial Agents / Q000037:antagonists & inhibitors / Q000494:pharmacology; D004352:Drug Resistance, Microbial; D004355:Drug Stability; D007709:Klebsiella / Q000187:drug effects / Q000201:enzymology; D007769:Lactams; D011514:Proteus vulgaris / Q000187:drug effects / Q000201:enzymology; D013053:Spectrophotometry; D001618:beta-Lactamases / Q000096:biosynthesis; D047090:beta-Lactams
D000900:Anti-Bacterial Agents; D007769:Lactams; D047090:beta-Lactams; C027318:nocardicin; D001618:beta-Lactamases