title: Enzymatic inactivation of a new aminoglycoside antibiotic, sisomicin by resistant strains of Pseudomonas aeruginosa.
abstract: The antibacterial activity of sisomicin (SS), a new aminoglycoside antibiotic active toward clinical isolates of Pseudomonas aeruginosa, was determined and compared with that of the gentamicin C complex. Both drugs were effective against these strains and showed almost the same antibacterial activity. A few strains were found to be resistant to SS. The antibiotic was inactivated by a cell-free extract from the SS-resistant strains due to acetylation of the drug. Comparative studies of the inactivation of the drugs which lack a 6'-amino group in the amino sugar linked to 2-deoxystreptamine strongly suggested that SS inactivation was due to acetylation of the 6'-amino group of the 4',5'-didehydropurpurosamine moiety.
authors.forename: K
authors.initials: K
authors.lastname: O'Hara
authors.forename: M
authors.initials: M
authors.lastname: Kono
authors.forename: S
authors.initials: S
authors.lastname: Mitsuhashi
mesh_terms: D000107:Acetylation; D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D002474:Cell-Free System; D024881:Drug Resistance, Bacterial; D004798:Enzymes / Q000378:metabolism; D011550:Pseudomonas aeruginosa / Q000187:drug effects* / Q000378:metabolism; D012853:Sisomicin / Q000494:pharmacology*
chemical_list: D000900:Anti-Bacterial Agents; D004798:Enzymes; D012853:Sisomicin