The Production of Gluconic Acid and 2-Keto-Gluconic Acid from Glucose by Species of
            <i>Pseudomonas</i>
            and
            <i>Phytomonas</i>

Lockwood, Lewis B.; Tabenkin, B.; Ward, George E.

doi:10.1128/jb.42.1.51-61.1941

Cited by 67 publications

(17 citation statements)

References 9 publications

(3 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Similar results were obtained for P. putida (formerly P. fluorescens) (5). Furthermore, exposure of fluorescent pseudomonads to high concentrations of glucose often results in quantitative conversion to gluconate (12). Moreover, Eisenberg et al (4) have presented evidence that although P. fluorescens can transport and phosphorylate glucose and oxidize the resulting glucose-6-phosphate to 6-phosphogluconate, this organism will not grow on glucose unless it is oxidized to gluconate which is required for induction of 6-phosphogluconate dehydratase (19).…”

Section: Discussionsupporting

confidence: 77%

Relationship between catabolism of glycerol and metabolism of hexosephosphate derivatives by Pseudomonas aeruginosa

Heath¹,

Gaudy²

1978

J Bacteriol

View full text Add to dashboard Cite

The relationship between catabolism of glycerol and metabolism of hexosephosphate derivatives in Pseudomonas aeruginosa was studied by comparing the growth on glycerol and enzymatic constitution of strain PAO with these characteristics of glucose-catabolic mutants and revertants. Growth of strain PAO on glycerol induced a catabolic oxidized nicotinamide adenine dinucleotide-linked glyceraldehyde-phosphate dehydrogenase and seven glucose-catabolic enzymes. The results indicated that these enzymes were induced by a six-carbon metabolite of glucose. All strains possessed a constitutive anabolic Embden-Meyerhof-Parnas pathway allowing limited conversion of glycerol-derived triosephosphate to hexosephosphate derivatives, which was consistent with induction of these enzymes by glycerol. Phosphogluconate dehydratase-deficient mutants grew on glycerol. However, mutants lacking both phosphogluconate dehydrogenase and phosphogluconate dehydratase were unable to grow on glycerol, although these strains possessed all of the enzymes needed for degradation of glycerol. These mutants apparently were inhibited by hexosephosphate derivatives, which originated from glycerol-derived triosephosphate and could not be dissimilated. This conclusion was supported by the fact that revertants regaining only a limited capacity to degrade 6-phosphogluconate were glycerol positive but remained glucose negative.

show abstract

Section: Discussionsupporting

confidence: 77%

Relationship between catabolism of glycerol and metabolism of hexosephosphate derivatives by Pseudomonas aeruginosa

Heath¹,

Gaudy²

1978

J Bacteriol

View full text Add to dashboard Cite

show abstract

“…Glucose metabolism in gram-negative bacteria can proceed via phosphorylation to glucose-6-phosphate or by direct oxidation to gluconate, catalyzed by membrane-bound glucose dehydrogenase (EC 1.1.99.17) (4,27). This enzyme was shown recently to belong to the class of quinoproteins which have pyrrolo-quinoline quinone (PQQ) as the prosthetic group (6,8).…”

mentioning

confidence: 99%

Energy transduction by electron transfer via a pyrrolo-quinoline quinone-dependent glucose dehydrogenase in Escherichia coli, Pseudomonas aeruginosa, and Acinetobacter calcoaceticus (var. lwoffi)

Schie¹,

Hellingwerf²,

Dijken³

et al. 1985

J Bacteriol

127

View full text Add to dashboard Cite

The coupling of membrane-bound glucose dehydrogenase (EC 1.1.99.17) to the respiratory chain has been studied in whole cells, cell-free extracts, and membrane vesicles of gram-negative bacteria. Several Escherichia coil strains synthesized glucose dehydrogenase apoenzyme which could be activated by the prosthetic group pyrrolo-quinoline quinone. The synthesis of the glucose dehydrogenase apoenzyme was independent of the presence of glucose in the growth medium. Membrane vesicles of E. coli, grown on glucose or succinate, oxidized glucose to gluconate in the presence of pyrrolo-quinoline quinone. This oxidation led to the generation of a proton motive force which supplied the driving force for uptake of lactose, alanine, and glutamate. Reconstitution of glucose dehydrogenase with limiting amounts of pyrrolo-quinoline quinone allowed manipulation of the rate of electron transfer in membrane vesicles and whole cells. At saturating levels of pyrrolo-quinoline quinone, glucose was the most effective electron donor in E. coli, and glucose oxidation supported secondary transport at even higher rates than oxidation of reduced phenazine methosulfate. Apoenzyme of pyrrolo-quinoline quinone-dependent glucose dehydrogenases with similar properties as the E. coli enzyme were found in Acinetobacter calcoaceticus (var. Iwoffi) grown aerobically on acetate and in Pseudomonas aeruginosa grown anaerobically on glucose and nitrate.on July 5, 2020 by guest http://jb.asm.org/ Downloaded from 494 van SCHIE ET AL.

show abstract

“…Of a number of species tested, only Pseudomonas ovali? formed D-gluconate in considerable amounts (Lockwood, Tabenkin & Ward, 1941). This finding may reflect the absence of a dehydrogenase capable of oxidizing D-gluconate further.…”

Section: Discussionmentioning

confidence: 94%

Carbon and sulphur utilization during growth of Pseudomonas fluorescens on potassium d-glucose 6-O-sulphate as the sole sulphur source

Fitzgerald¹,

Dodgson²

1971

Biochemical Journal

View full text Add to dashboard Cite

Pseudomonas fluorescens N.C.I.B. 8248, cultured on potassium d-glucose 6[(35)S]-O-sulphate as the sole sulphur source, liberated the 6-O-sulphate ester of d-gluconate into the culture medium. Extracts of bacteria grown under this cultural condition oxidized d-glucose 6-O-sulphate to yield the gluconate ester. Results suggest the involvement of a glucose dehydrogenase-like enzyme. The gluconate ester was apparently not oxidized further to any significant extent; however, it served as substrate for a desulphating enzyme found in extracts. Growth on d-glucose 6-O-sulphate as the sole source of sulphur was not associated with the appearance of a true glycosulphatase. Collectively, these results suggest that d-gluconate 6-O-sulphate, rather than the glucose ester, supplied the necessary sulphur for growth. Oxidative activities toward d-glucose 6-O-sulphate, d-glucose, d-gluconate 6-O-sulphate and d-gluconate found in extracts of P. fluorescens adapted to grow on d-glucose 6-O-sulphate as the sole source of carbon and sulphur are presented for comparative purposes.

show abstract

The Production of Gluconic Acid and 2-Keto-Gluconic Acid from Glucose by Species of Pseudomonas and Phytomonas

Cited by 67 publications

References 9 publications

Relationship between catabolism of glycerol and metabolism of hexosephosphate derivatives by Pseudomonas aeruginosa

Relationship between catabolism of glycerol and metabolism of hexosephosphate derivatives by Pseudomonas aeruginosa

Energy transduction by electron transfer via a pyrrolo-quinoline quinone-dependent glucose dehydrogenase in Escherichia coli, Pseudomonas aeruginosa, and Acinetobacter calcoaceticus (var. lwoffi)

Carbon and sulphur utilization during growth of Pseudomonas fluorescens on potassium d-glucose 6-O-sulphate as the sole sulphur source

Contact Info

Product

Resources

About