Glycerol Utilization by Schizosaccharomyces pombe: Phosphorylation of Dihydroxyacetone by a Specific Kinase as the Second Step
John W. May, John Marshall, J. Sloan
Abstract
John W. May, John Marshall, J. Sloan
Abstract
Crude cell extracts of the fission yeast Schizosaccharomyces pombe (strains NCYC 132 and 972h−) can phosphorylate dihydroxyacetone but not glycerol; activity for dl-glyceraldehyde is very low. This suggests that a specific dihydroxyacetone kinase is present and catalyses the second step in a pathway for glycerol utilization, in which the initial step is an oxidation by an NAD+-linked glycerol dehydrogenase. In support of this pathway (glycerol→dihydroxyacetone→dihydroxyacetone phosphate), both strains can utilize glycerol or dihydroxyacetone. but not dl-glyceraldehyde, as growth substrates. Both enzymes are subject to catabolite repression and may also be inducible but are not co-ordinately regulated.
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Crude cell extracts of the fission yeast Schizosaccharomyces pombe (strains NCYC 132 and 972h−) can phosphorylate dihydroxyacetone but not glycerol; activity for dl-glyceraldehyde is very low. This suggests that a specific dihydroxyacetone kinase is present and catalyses the second step in a pathway for glycerol utilization, in which the initial step is an oxidation by an NAD+-linked glycerol dehydrogenase. In support of this pathway (glycerol→dihydroxyacetone→dihydroxyacetone phosphate), both strains can utilize glycerol or dihydroxyacetone. but not dl-glyceraldehyde, as growth substrates. Both enzymes are subject to catabolite repression and may also be inducible but are not co-ordinately regulated.
Key concepts: Dihydroxyacetone, Glycerol kinase, Dihydroxyacetone phosphate, Schizosaccharomyces pombe, Glyceraldehyde, Glycerol, Biochemistry, Dehydrogenase