Premium
Nature of Monocyclic β‐Lactam Antibiotic Nocardicin A to β‐Lactamases
Author(s) -
Kojo Hitoshi,
Mine Yasuhiro,
Nishida Minoru,
Goto Sachiko,
Kuwahara Shogo
Publication year - 1988
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.1988.tb01371.x
Subject(s) - cefoxitin , klebsiella oxytoca , lactam , proteus vulgaris , antibiotics , aztreonam , cephalosporin , beta lactam , moxalactam , biology , enzyme , beta lactamase inhibitors , microbiology and biotechnology , stereochemistry , chemistry , biochemistry , enterobacteriaceae , bacteria , antibacterial activity , antibiotic resistance , escherichia coli , genetics , staphylococcus aureus , imipenem , gene
Nocardicin A is the antibiotic which was first found to possess a monocyclic β‐lactam ring. This antibiotic was inactivated by the cleavage of its β‐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 β‐lactamases. Of the nine β‐lactam antibiotics including cefoxitin and cefuroxime, Nocardicin A was the most stable to the β‐lactamases tested excluding those from Klebsiella oxytoca and Proteus vulgaris. The latter broad‐spectrum β‐lactamases hydrolyzed Nocardicin A rather intensively. Extreme stability of Nocardicin A to β‐lactamases was suggested to be due to the combination of its low affinity to the enzymes and stabilization of its monocyclic β‐lactam ring. Nocardicin A was shown to have inducing ability toward β‐lactamases.