D-Mannitol oxidation in the land snail, Helix aspersa.
Respiration by mitochondrial preparations from hepatopancreas tissue of the land snail Helix aspersa is stimulated by D-mannitol. The rate of mannitol-stimulated respiration is approximately one-half that given by succinate, the most effective substrate thus far tested with these preparations. Mannitol-stimulated respiration is cyanide-insensitive but is not inhibited by salicylhydroxamate. The product of the membrane-bound mannitol-oxidizing activity was shown to be D-mannose by thin layer chromatography, high voltage electrophoresis of the germanate and borate complexes, gas chromatography of the trimethylsilyl derivative, low resolution mass spectrometry of the trimethylsilyl derivative, and by an enzymatic method dependent upon phosphomannose isomerase. The reaction mannitol + O2 leads to mannose is stoichiometric; however, it is not known whether O2 is the immediate electron acceptor. The activity in Helix mitochondria is thus unique among most alditol-oxidizing enzymes in not being pyridine nucleotide linked and in acting on carbon 1 rather than carbon 2.
D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D000818:Animals; D002849:Chromatography, Gas; D003576:Electron Transport Complex IV / Q000378:metabolism; D006372:Helix, Snails / Q000378:metabolism*; D008353:Mannitol / Q000378:metabolism*; D013058:Mass Spectrometry; D008928:Mitochondria / Q000378:metabolism; D010084:Oxidation-Reduction; D010101:Oxygen Consumption; D013386:Succinates / Q000378:metabolism; D013402:Sugar Alcohols / Q000378:metabolism
D013386:Succinates; D013402:Sugar Alcohols; D008353:Mannitol; D000429:Alcohol Oxidoreductases; D003576:Electron Transport Complex IV