Respiratory behaviour of a Zymomonas mobilis adhB::kan(r) mutant supports the hypothesis of two alcohol dehydrogenase isoenzymes catalysing opposite reactions
| Autor: | Uldis Kalnenieks, Robert K. Poole, James L. Pickford, Nina Galinina, Reinis Rutkis, M. Toma |
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| Rok vydání: | 2006 |
| Předmět: |
Kanamycin Resistance
Biophysics Metabolic channelling Chemostat Biochemistry Redox Zymomonas mobilis Models Biological Catalysis chemistry.chemical_compound Continuous culture Structural Biology Genetics Ethanol metabolism Molecular Biology Alcohol dehydrogenase Zymomonas Ethanol biology Chemistry Respiration Acetaldehyde Alcohol Dehydrogenase Cell Biology biology.organism_classification Aerobiosis Isoenzymes Kinetics biology.protein Mutant Proteins NAD+ kinase |
| Zdroj: | FEBS letters. 580(21) |
| ISSN: | 0014-5793 |
| Popis: | Perturbation of the aerobic steady-state in a chemostat culture of the ethanol-producing bacterium Zymomonas mobilis with a small pulse of ethanol causes a burst of ethanol oxidation, although the reactant ratio of the alcohol dehydrogenase (ADH) reaction ([NADH][acetaldehyde][H+])/([ethanol][NAD+]) remains above the Keq value. Simultaneous catalysis of ethanol synthesis and oxidation by the two ADH isoenzymes, residing in different redox microenvironments, has been proposed previously. In the present study, this hypothesis is verified by construction of an ADH-deficient strain and by demonstration that it lacks the oxidative burst in response to perturbation of its aerobic steady-state with ethanol. |
| Databáze: | OpenAIRE |
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