Glyceraldehyde phosphate dehydrogenase activity with triphosphopyridine nucleotide and with diphosphopyridine nucleotide.

The results presented here are part of a study of pentose synthesis in Alcaligenes fuecalis. The mechanism of pentose synthesis is of interest since the organism can synthesize pentose from acetate, but cannot use hexoses for growth (1). In the course of the investigation into the enzymes associated with this synthesis, glyceraldehyde phosphate dehydrogenase activity, with either triphosphopyridine nucleotide or diphosphopyridine nucleotide as coenzyme, was observed. The activity of the enzyme with triphosphopyridine nucleotide as coenzyme suggested that this enzyme was different from the yeast and muscle dehydrogenases, but similar to the plant triphosphopyridine nucleotide-linked enzyme. This paper describes the purification and properties of the glyceraldehyde 3-phosphate dehydrogenase from A. fuecalis.