6533b7d5fe1ef96bd1263e71

RESEARCH PRODUCT

Respiratory behaviour of a Zymomonas mobilis adhB::kan(r) mutant supports the hypothesis of two alcohol dehydrogenase isoenzymes catalysing opposite reactions.

Uldis KalnenieksRobert K. PooleJames L. PickfordNina GalininaReinis RutkisM. Toma

subject

Kanamycin ResistanceBiophysicsMetabolic channellingChemostatBiochemistryRedoxZymomonas mobilisModels BiologicalCatalysischemistry.chemical_compoundContinuous cultureStructural BiologyGeneticsEthanol metabolismMolecular BiologyAlcohol dehydrogenaseZymomonasEthanolbiologyEthanolChemistryRespirationZymomonas mobilisAcetaldehydeAlcohol DehydrogenaseCell Biologybiology.organism_classificationAerobiosisIsoenzymesKineticsBiochemistrybiology.proteinMutant ProteinsNAD+ kinase

description

AbstractPerturbation 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.

yearjournalcountryeditionlanguage
2006-07-10FEBS letters
10.1016/j.febslet.2006.08.034https://pubmed.ncbi.nlm.nih.gov/16950260