Does aminoglycoside-acetyltransferase in rapidly growing mycobacteria have a metabolic function in addition to aminoglycoside inactivation?
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.
Udou
T
T
Department of Microbiology, School of Medicine, University of Occupational and Environmental Health, Kitakyushu, Japan.
Mizuguchi
Y
Y
Wallace
R J
RJ
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
D000617:Aminoglycosides; D000900:Anti-Bacterial Agents; D010071:Oxaloacetates; D000123:Acetyltransferases; C019681:aminoglycoside acetyltransferase