Summary: The fission yeast has been shown to produce four separate pyridine nucleotide-linked glycerol dehydrogenases (or triose reductases), distinguished by differences in their coenzyme specificity (NAD or NADP) and oxidation product (dihydroxyacetone or glyceraldehyde). Evidence for four separate activities was obtained by heat inactivation studies, comparison of cells grown under different conditions, and separation and partial purification of the enzymes. One enzyme, a glycerol: NAD 2-oxidoreductase is repressed by glucose but not induced by glycerol and appears to function primarily in glycerol catabolism. The second, a glycerol: NADP 2-oxidoreductase is stimulated by growth on glucose and appears to function as a dihydroxyacetone reductase involved in glycerol synthesis. The third has the properties of a glycerol: NADPT oxidoreductase, while the fourth is, in fact, alcohol dehydrogenase (alcohol: NAD oxidoreductase) which possesses weak activity as a glycerol: NAD 1-oxidoreductase.


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