Unique alcohol dehydrogenases involved in algal sugar utilization by marine bacteria [PDF]
Applied Microbiology and Biotechnology, 2023 Abstract Marine algae produce complex polysaccharides, which can be degraded by marine heterotrophic bacteria utilizing carbohydrate-active enzymes. The red algal polysaccharide porphyran contains the methoxy sugar 6-O-methyl-d-galactose (G6Me).
Stefan Brott +9 more
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Extended superfamily of short alcohol‐polyol‐sugar dehydrogenases: structural similarities between glucose and ribitol dehydrogenases [PDF]
FEBS Letters, 1984 The recently determined primary structure of glucose dehydrogenase from Bacillus megaterium was scanned by computerized comparisons for similarities with known polyol and alcohol dehydrogenases. The results revealed a highly significant similarity between this glucose dehydrogenase and ribitol dehydrogenase from Klebsiella aerogenes.
Hans Jörnvall +4 more
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Changes in Soluble Sugar, Starch, and Alcohol Dehydrogenase in Arabidopsis thaliana Exposed to N2 Diluted Atmospheres [PDF]
Plant and Cell Physiology, 1997 Proper exchange of atmospheric gases is important for normal root and shoot metabolism in plants. This study was conducted to determine how restricted air supply affects foliar carbohydrates, while using the marker enzyme alcohol dehydrogenase (ADH) to report on the oxygenation status of the rootzone.
D. Marshall Porterfield +2 more
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Membrane-bound Sugar Alcohol Dehydrogenase in Acetic Acid Bacteria catalyzes L-Ribulose Formation and NAD-Dependent Ribitol Dehydrogenase is Independent of the Oxidative Fermentation [PDF]
Bioscience, Biotechnology, and Biochemistry, 2001 To identify the enzyme responsible for pentitol oxidation by acetic acid bacteria, two different ribitol oxidizing enzymes, one in the cytosolic fraction of NAD(P)-dependent and the other in the membrane fraction of NAD(P)-independent enzymes, were examined with respect to oxidative fermentation.
Osao Adachi +8 more
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Gametophytic Variant of Alcohol Dehydrogenase ADH-P in Sugar Beet: Inheritance and Influence on Pseudo-Compatibility [PDF]
Hereditas, 2004 A gametophytic variant ADH-P (alcohol dehydrogenase in pollen) was found in one plant in the sugar beet inbred line C257c. It was found only in developing and mature pollen, attempts failed to find it in other tissues. Rather than as an independent protein, ADH-P appeared as a variant of the ADH protein, accompanying the main proteins ADH1-FF and ADH1 ...
Alexander A. Konovalov
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Comprehensive Comparative Genomics and Phenotyping of Methylobacterium Species
Frontiers in Microbiology, 2021 The pink-pigmented facultative methylotrophs (PPFMs), a major bacterial group found in the plant phyllosphere, comprise two genera: Methylobacterium and Methylorubrum. They have been separated into three major clades: A, B (Methylorubrum), and C.
Ola Alessa +6 more
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Biotechnology for Biofuels, 2021 Background Fungal glucose dehydrogenases (GDHs) are FAD-dependent enzymes belonging to the glucose-methanol-choline oxidoreductase superfamily. These enzymes are classified in the “Auxiliary Activity” family 3 (AA3) of the Carbohydrate-Active enZymes ...
Gabriele Cerutti +13 more
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Microbial Cell Factories, 2021 Background Xylitol is a five-carbon sugar alcohol that has numerous beneficial health properties. It has almost the same sweetness as sucrose but has lower energy value compared to the sucrose.
Tai Man Louie +6 more
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Genome-wide analysis of the UDP-glucose dehydrogenase gene family in Arabidopsis, a key enzyme for matrix polysaccharides in cell walls [PDF]
, 2007 Arabidopsis cell walls contain large amounts of pectins and hemicelluloses, which are predominantly synthesized via the common precursor UDP-glucuronic acid.
Klinghammer, Michaela, Tenhaken, Raimund
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Optimization of Enzymatic Gas-Phase Reactions by Increasing the Long-Term Stability of the Catalyst [PDF]
, 2004 Enzymatic gas-phase reactions are usually performed in continuous reactors, and thus very stable and active catalysts are required to perform such transformations on cost-effective levels.
Büchs, Jochen, +4 more
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