Abstract
The antibacterial activity, binding to penicillin-binding proteins, and morphological changes effected by YTR 830, a sulfone beta-lactamase inhibitor, were studied in comparison with those of other beta-lactamase inhibitors. YTR 830 had very poor antibacterial activity, bound to PBP 2 of gram-negative organisms, and at the MIC caused rapid lysis of spheroplasts formed.
MeSH Terms
Bacteria/drug effects,ultrastructure
Bacterial Proteins
Carrier Proteins/metabolism
Clavulanic Acids/pharmacology
Hexosyltransferases
Microbial Sensitivity Tests
Muramoylpentapeptide Carboxypeptidase/metabolism
Penicillanic Acid/pharmacology
Penicillin-Binding Proteins
Peptidyl Transferases
Sulbactam/pharmacology
Tazobactam
beta-Lactamase Inhibitors
Chemicals
Bacterial Proteins
Carrier Proteins
Clavulanic Acids
Penicillin-Binding Proteins
beta-Lactamase Inhibitors
Penicillanic Acid
Peptidyl Transferases
Hexosyltransferases
Muramoylpentapeptide Carboxypeptidase
Sulbactam
Tazobactam
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Moosdeen F
Department of Medical Microbiology, London Hospital Medical College, England.
Williams J D
Yamabe S
References (13)
13 references, click to expand
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