flavin-adenine-dinucleotide and gluconic-acid

flavin-adenine-dinucleotide has been researched along with gluconic-acid* in 3 studies

Other Studies

3 other study(ies) available for flavin-adenine-dinucleotide and gluconic-acid

ArticleYear
Membrane-bound, 2-keto-D-gluconate-yielding D-gluconate dehydrogenase from "Gluconobacter dioxyacetonicus" IFO 3271: molecular properties and gene disruption.
    Applied and environmental microbiology, 2007, Volume: 73, Issue:20

    Most Gluconobacter species produce and accumulate 2-keto-d-gluconate (2KGA) and 5KGA simultaneously from d-glucose via GA in culture medium. 2KGA is produced by membrane-bound flavin adenine dinucleotide-containing GA 2-dehydrogenase (FAD-GADH). FAD-GADH was purified from "Gluconobacter dioxyacetonicus" IFO 3271, and N-terminal sequences of the three subunits were analyzed. PCR primers were designed from the N-terminal sequences, and part of the FAD-GADH genes was cloned as a PCR product. Using this PCR product, gene fragments containing whole FAD-GADH genes were obtained, and finally the nucleotide sequence of 9,696 bp was determined. The cloned sequence had three open reading frames (ORFs), gndS, gndL, and gndC, corresponding to small, large, and cytochrome c subunits of FAD-GADH, respectively. Seven other ORFs were also found, one of which showed identity to glucono-delta-lactonase, which might be involved directly in 2KGA production. Three mutant strains defective in either gndL or sldA (the gene responsible for 5KGA production) or both were constructed. Ferricyanide-reductase activity with GA in the membrane fraction of the gndL-defective strain decreased by about 60% of that of the wild-type strain, while in the sldA-defective strain, activity with GA did not decrease and activities with glycerol, d-arabitol, and d-sorbitol disappeared. Unexpectedly, the strain defective in both gndL and sldA (double mutant) still showed activity with GA. Moreover, 2KGA production was still observed in gndL and double mutant strains. 5KGA production was not observed at all in sldA and double mutant strains. Thus, it seems that "G. dioxyacetonicus" IFO 3271 has another membrane-bound enzyme that reacts with GA, producing 2KGA.

    Topics: Amino Acid Sequence; Carbohydrate Dehydrogenases; Cell Membrane; Flavin-Adenine Dinucleotide; Gluconates; Gluconobacter; Molecular Sequence Data; Mutation; Polymerase Chain Reaction; Sequence Analysis, DNA

2007
Preparation of enzymes required for enzymatic quantification of 5-keto-D-gluconate and 2-keto-D-gluconate.
    Bioscience, biotechnology, and biochemistry, 2007, Volume: 71, Issue:10

    For easy measurement of 5-keto D-gluconate (5KGA) and 2-keto D-gluconate (2KGA), two enzymes, 5KGA reductase (5KGR) and 2KGA reductase (2KGR) are useful. The gene for 5KGR has been reported, and a corresponding gene was found in the genome of Gluconobacter oxydans 621H and was identified as GOX2187. On the other hand, the gene for 2KGR was identified in this study as GOX0417 from the N-terminal amino acid sequence of the partially purified enzyme. Several plasmids were constructed to express GOX2187 and GOX0417, and the final constructed plasmids showed good expression of 5KGR and 2KGR in Escherichia coli. From the two E. coli transformants, large amounts of each enzyme were easily prepared after one column chromatography, and the preparation was ready to use for quantification of 5KGA or 2KGA.

    Topics: Amino Acid Sequence; Carbohydrate Dehydrogenases; Cloning, Molecular; Enzyme Stability; Escherichia coli; Flavin-Adenine Dinucleotide; Genes, Bacterial; Gluconates; Gluconobacter; Models, Biological; Molecular Sequence Data; Mutation; Plasmids; Sequence Homology, Amino Acid; Substrate Specificity; Time Factors; Transformation, Genetic

2007
Supramolecular architectures of electrostatic self-assembled glucose oxidase enzyme electrodes.
    Chemphyschem : a European journal of chemical physics and physical chemistry, 2004, Feb-20, Volume: 5, Issue:2

    Topics: Biosensing Techniques; Catalysis; Electrodes; Enzymes, Immobilized; Flavin-Adenine Dinucleotide; Gluconates; Glucose; Glucose Oxidase; Kinetics; Membranes, Artificial; Oxidation-Reduction; Polyamines; Potentiometry

2004