Myo-inositol dehydrogenase(s) from Acetomonas oxydans.
Experimental studies have been undertaken with a view of isolation of the enzyme(s) responsible for the stereospecific oxidation of myo-inositol. A partial fractionation has been achieved and the properties of this extract examined. Results show that the active enzyme may well have a cytochrome component and there is indication that the stereospecificity of Acetomonas oxydans results from permease as opposed to dehydrogenase activity. Kinetic experiments suggest that only one type of active enzyme site is involved in the dehydrogenation of myo-inositol.
D015086:2,6-Dichloroindophenol / Q000378:metabolism; D000429:Alcohol Oxidoreductases / Q000032:analysis / Q000378:metabolism; D001426:Bacterial Proteins / Q000032:analysis; D002458:Cell Fractionation; D003580:Cytochromes / Q000032:analysis; D007294:Inositol / Q000378:metabolism; D008970:Molecular Weight; D010084:Oxidation-Reduction; D010101:Oxygen Consumption; D011548:Pseudomonadaceae / Q000201:enzymology*; D013237:Stereoisomerism
D001426:Bacterial Proteins; D003580:Cytochromes; D007294:Inositol; D015086:2,6-Dichloroindophenol; D000429:Alcohol Oxidoreductases