Complete genome sequence of the acetic acid bacterium Gluconobacter oxydans

Prust, Christina; Hoffmeister, Marc; Liesegang, Heiko; Wiezer, Arnim; Fricke, W. Florian; Ehrenreich, Armin; Gottschalk, Gerhard; Deppenmeier, Uwe

doi:10.1038/nbt1062

Cited by 392 publications

(365 citation statements)

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“…This quinoprotein is considered the main polyol-dehydrogenase of G. oxydans that exhibits a broad substrate specificity. It catalyzes the oxidation of D-sorbitol, gluconate, and glycerol to L-sorbose, 5-ketogluconate and DHA, respectively [54].…”

Section: Carbon Sourcesmentioning

confidence: 99%

Acetic Acid Bacteria: Physiology and Carbon Sources Oxidation

2013

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Acetic acid bacteria (AAB) are obligately aerobic bacteria within the family Acetobacteraceae, widespread in sugary, acidic and alcoholic niches. They are known for their ability to partially oxidise a variety of carbohydrates and to release the corresponding metabolites (aldehydes, ketones and organic acids) into the media. Since a long time they are used to perform specific oxidation reactions through processes called ''oxidative fermentations'', especially in vinegar production. In the last decades physiology of AAB have been widely studied because of their role in food production, where they act as beneficial or spoiling organisms, and in biotechnological industry, where their oxidation machinery is exploited to produce a number of compounds such as L-ascorbic acid, dihydroxyacetone, gluconic acid and cellulose. The present review aims to provide an overview of AAB physiology focusing carbon sources oxidation and main products of their metabolism.

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Section: Carbon Sourcesmentioning

confidence: 99%

Acetic Acid Bacteria: Physiology and Carbon Sources Oxidation

2013

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“…The molecular size of the MGL purified in this study was inconsistent with the genomic information deduced, that gene gnlA carrying D-glucono--lactonase in the periplasm was composed of 342 amino acid residues. 26) Gel filtration with Sephadex columns 27) confirmed that MGL might have the molecular weight of 120k, implying that MGL might be composed of two identical subunits. MGL showed a clear contrast to SGL when the physicochemical and catalytic properties were compared ( Table 2).…”

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confidence: 99%

Solubilization, Purification, and Properties of Membrane-BoundD-Glucono-δ-lactone Hydrolase fromGluconobacter oxydans

Shinagawa

Ano

Yakushi

et al. 2009

Bioscience, Biotechnology, and Biochemistry

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“…The first description of the mALDH structure in G. oxydans by Adachi et al 1980 revealed the presence of two distinct subunits, a major subunit 86 kDa and a minor subunit 55 kDa 12 . However, a more recent analysis of the respective mALDH components in G. oxydans 13 revealed the presence of three distinct subunits, encoded by three consecutive open reading frames GOX0585-GOX0587 . Using the mALDH complex from Acetobacter europaeus as a template, subunits GOX0585, GOX0586, and GOX0587 were designated aldF cytochrome c subunit , aldG small subunit , and aldH large subunit 14 , respectively.…”

mentioning

confidence: 99%