Oxidative Dissimilation in Pantothenate-Deficient Acetobacter suboxydans Cells.

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Abstract
Resting deficient cells show retarded ability to oxidase dihydroxy-acetone, sorbose, and gluconic acid, and somewhat poorer ability to convert sorbitol to sorbose. Addition of coenzyme A to the deficient cells significantly improves their ability to oxidize dihydroxyacetone, thus suggesting that the further dissimilation of this substrate is coenzyme A-linked. The oxidation of alcohol, of glycerol to dihydroxyacetone, and of glucose to gluconic acid indicated non-involvement of coenzyme A in these reactions.