Oxidation of dihydroxyacetone via the pentose cycle in Acetobacter sub-oxydans.

Acetobacter suboxydans has for many years been regarded as an organism possessing broad but limited ability to attack sugars and other polyhydroxy compounds (1). More recently, it has become apparent that the organism possesses a number of enzymes for more extensive dissimilation of substrates such as glucose, glycerol, and sorbitol (2). On the other hand, diand tricarboxylic acid cycle activities appear to be absent in this organism (3), and several important components of the normal Embden-Meyerhof pathway are also lacking. In the present work attention has been focused on dihydroxyacetone’ in an attempt to trace its fate in the oxidative machinery of the cell. In order to study individual reactions and to allow the free access of phosphorylated intermediates to enzyme surfaces, the organization of the whole cells was in nearly all experiments sacrificed and soluble cell-free extracts were employed.