title: Does aminoglycoside-acetyltransferase in rapidly growing mycobacteria have a metabolic function in addition to aminoglycoside inactivation?
abstract: All the rapidly growing mycobacteria tested, Mycobacterium fortuitum complex, M. smegmatis, M. phlei, and M. vaccae, contained one of two characteristics, but were different from previously recognized aminoglycoside-acetyltransferases. The acetylation reaction of both the enzymes from M. fortuitum and Pseudomonas aeruginosa (3-N-acetyltransferase-III) with radiolabeled acetyl coenzyme A was inhibited severely by oxalacetate. It was suggested that the inhibitory effect of oxalacetate is due to the condensation reaction between oxalacetate and acetyl coenzyme A resulting in the generation of citrate.
authors.affiliation: Department of Microbiology, School of Medicine, University of Occupational and Environmental Health, Kitakyushu, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Udou
authors.forename: Y
authors.initials: Y
authors.lastname: Mizuguchi
authors.forename: R J
authors.initials: RJ
authors.lastname: Wallace
mesh_terms: D000123:Acetyltransferases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000617:Aminoglycosides; D000900:Anti-Bacterial Agents / Q000037:antagonists & inhibitors / Q000494:pharmacology; D004352:Drug Resistance, Microbial; D009161:Mycobacterium / Q000187:drug effects / Q000254:growth & development / Q000378:metabolism*; D010071:Oxaloacetates / Q000494:pharmacology; D011550:Pseudomonas aeruginosa / Q000201:enzymology; D013379:Substrate Specificity
chemical_list: D000617:Aminoglycosides; D000900:Anti-Bacterial Agents; D010071:Oxaloacetates; D000123:Acetyltransferases; C019681:aminoglycoside acetyltransferase