title: Metabolic consequences of a block in the synthesis of 5-keto-D-fructose in a mutant of Gluconobacter cerinus.
abstract: A mutant of Gluconobacter cerinus var. ammoniacus, IFO 3267, has been isolated which is deficient with respect to fructose 5-dehydrogenase, the enzyme catalyzing the oxidation of d-fructose to 5-keto-d-fructose (5 KF). Growth of this mutant on fructose as the sole carbon source was impaired unless the culture medium was supplemented with 5 KF. Significant randomization of the 1 and 6 positions of fructose has been reported previously for the wild-type organism during growth on this ketohexose. The pattern of (3)H incorporation into the C5 position of ribonucleic acid-ribose when the mutant was grown on [1-(3)H]fructose and [6-(3)H]fructose in the presence of 5 KF indicated that such randomization did not occur in this variant. The randomization observed in the wild type is, therefore, a consequence of the partial oxidation of fructose to the symmetrical 5 KF intermediate prior to its conversion to pentose. When the mutant was grown on [1-(3)H]fructose in the presence of unlabeled 5 KF, [5-(3)H]fructose appeared in the culture medium. Thus, 5 KF served as the oxidant for the nicotinamide adenine dinucleotide phosphate, reduced form, generated during growth on fructose.
mesh_terms: D000429:Alcohol Oxidoreductases / Q000096:biosynthesis* / Q000378:metabolism; D001419:Bacteria / Q000201:enzymology / Q000378:metabolism*; D002250:Carbon Radioisotopes; D002474:Cell-Free System; D002854:Chromatography, Paper; D005632:Fructose / Q000378:metabolism; D005956:Glucose-6-Phosphate Isomerase / Q000378:metabolism; D007661:Ketoses / Q000096:biosynthesis*; D009153:Mutagens; D009154:Mutation; D009604:Nitrosoguanidines; D012266:Ribose / Q000096:biosynthesis; D013237:Stereoisomerism; D014316:Tritium
chemical_list: D002250:Carbon Radioisotopes; D007661:Ketoses; D009153:Mutagens; D009604:Nitrosoguanidines; D014316:Tritium; D005632:Fructose; D012266:Ribose; D000429:Alcohol Oxidoreductases; D005956:Glucose-6-Phosphate Isomerase