Purification and Characterization of Two NAD-Dependent Alcohol Dehydrogenases (ADHs) Induced in the Quinoprotein ADH-Deficient Mutant ofAcetobacter pasteurianusSKU1108

A Novel 3-Dehydroquinate Dehydratase Catalyzing Extracellular Formation of 3-Dehydroshikimate by Oxidative Fermentation ofGluconobacter oxydansIFO 3244

“…8) When DQD activity was surveyed with membrane fractions of certain Gluconobacter strains, pDQD was detected only with strains accommodating QDH in the membrane fraction, although detectable enzyme activity of sDQD was found in the cytoplasmic fraction of all strains examined. The ratio of pDQD in the membrane fraction to sDQD in the cytoplasmic fraction was similar to other examples such as quinoprotein alcohol dehydrogenase in the membrane fraction to NAD-dependent alcohol dehydrogenase in the cytoplasmic fraction of acetic acid bacteria, [15][16][17] and membrane-bound quinoprotein cyclic alcohol dehydrogenase to NAD-dependent cyclic alcohol dehydrogenase.…”

“…These results indicte that sDQD occupied 0.025% of the total protein of the cell-free extract, similarly to the existence of other cytoplasmic enzymes in acetic acid bacteria. [15][16][17][18] The magnification of enzyme purification and the final yield were almost at the same level as DQD in E. coli.…”

Transcriptome response to different carbon sources in Acetobacter aceti

“…The largest subunit gene (adhA) and the cytochrome c subunit gene (adhB) were clustered, but the smallest subunit gene (adhC) was separated as in the cases of other acetic acid bacteria (Kondo & Horinouchi, 1997;Tamaki et al, 1991). The adh1 and adh2 genes for soluble NAD + -dependent ADHs corresponding to ADH I and ADH II of A. pasteurianus SKU1108, respectively (Chinnawirotpisan et al, 2003), were also identified. They were expected to be involved in oxidation of ethanol in the cytoplasm.…”

Purification and Properties of Two Different Dihydroxyacetone Reductases inGluconobacter suboxydansGrown on Glycerol

“…Such a high occurrence of NAD(P)-dependent enzyme is sometimes seen even in acetic acid bacteria. 24,33,36,37) Crystallization of the two different DHARs was done batchwise with AS, and fine needle crystals forming hexagrams appeared with NADPH-DHAE (Fig. 2) as well as the formation of fine needles with NADH-DHAR, as shown in Fig.…”

“…Ethanol-grown cells of Acetobacter and Gluconobacter strains show strong ethanol-oxidizing activity with the membrane fraction, while only a little enzyme activity of cytoplasmic NAD(P)-dependent alcohol dehydrogenase is observed. 24) When membrane-bound quinoprotein alcohol dehydrogenase (QADH) is deleted by means of genetic mutation, QADH disappears from the membrane fraction and cytoplasmic NAD(P)-dependent alcohol dehydrogenase activities increase remarkably. Acetate production with such a mutant no longer takes place and total cell growth increases, because the ethanol added to the culture medium is fully converted to carbon and energy sources for the mutant.…”