Binding of a non- β -lactam antibiotic to penicillin-binding proteins

• Published in: Nature (London) 1987-01, Vol.325 (6100), p.179-180
• Main Authors: Nozaki, Y, Katayama, N, Ono, H, Tsubotani, S, Harada, S, Okazaki, H, Nakao, Y
• Format: Article
• Language: English
• Subjects: Anti-Bacterial Agents - metabolism; Antibiotics (antibacterial agents, antifungal agents); Antibiotics, microbial producers, chemotherapic agents, antiseptics, disinfecting agents; Applied microbiology; Bacterial Proteins; Binding, Competitive; Biological and medical sciences; Carrier Proteins - metabolism; Escherichia coli; Fundamental and applied biological sciences. Psychology; Hexosyltransferases; Humanities and Social Sciences; letter; Microbial Sensitivity Tests; Microbiology; multidisciplinary; Muramoylpentapeptide Carboxypeptidase - metabolism; Penicillin-Binding Proteins; Peptides; Peptides, Cyclic - metabolism; Peptidyl Transferases; Protein Binding; Science; Science (multidisciplinary)
• ISSN: 0028-0836; 1476-4687
• DOI: 10.1038/325179a0

In the search for new β -lactam antibiotics of natural origin, the discoveries of cephamycins 1 and sulfazecins 2 (monobactams 3 ) were important turning points in that they accelerated many screening efforts aimed at other new compounds. In our target-directed screening for β -lactam antibiotics using β -lactam hypersensitive mutants 4,5 , we have examined Gram-negative bacteria isolated from natural habitats and have recently reported several types of β -lactam antibiotics such as cephabacins 6,7 and formadicins 8 . Here we report a novel antibiotic, lactivicin, found using this system. Although lactivicin has various biological activities commonly observed in β -lactam antibiotics, it does not possess a β -lactam ring in its molecule, but has the unique structure of a dicyclic dipeptide.