Does aminoglycoside-acetyltransferase in rapidly growing mycobacteria have a metabolic function in addition to aminoglycoside inactivation?
| Autor: | Takezo Udou, Richard J. Wallace, Yasuo Mizuguchi |
|---|---|
| Rok vydání: | 1989 |
| Předmět: |
Oxaloacetates
Biology medicine.disease_cause Microbiology Mycobacterium Substrate Specificity Acetyltransferases Genetics medicine Molecular Biology chemistry.chemical_classification Pseudomonas aeruginosa Aminoglycoside Drug Resistance Microbial bacterial infections and mycoses biology.organism_classification Mycobacterium fortuitum Complex Anti-Bacterial Agents Aminoglycosides Enzyme Biochemistry chemistry Acetylation Acetyltransferase Mycobacterium fortuitum |
| Zdroj: | FEMS Microbiology Letters. 57:227-230 |
| ISSN: | 0378-1097 |
| DOI: | 10.1111/j.1574-6968.1989.tb03304.x |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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