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Cell free extracts of Acetobacter suboxydans catalyze the formation of triosephosphate from either glucose or glycerol. The same extracts consume triosephosphate by the aldolase and pentose cycle reactions (Hauge et al., 1955; Kitos, 1956). Although fructose-1 , 6-diphosphate (FDP)3 is oxidized by molecular oxygen in the presence of either whole cells or cell extract, other evidence does not indicate that glycolysis operates to a significant degree in this organism (King and Cheldelin, 1954). This paper is concerned with the conversion of FDP to 3-phosphoglyceric acid (3-PGA)3 and the further metabolism of this substrate as far as the products of acetate activation. The conditions under which these glycolytic enzymes function differentiate them from those commonly observed in other cells.

METABOLISM OF FRUCTOSE-1,6-DIPHOSPHATE AND ACETATE IN ACETOBACTER SUBOXYDANS