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Summary: Dihydroxyacetone kinase (ATP: dihydroxyacetone phosphotransferase) from Schizosaccharomyces pombe has been purified and characterized. It has an M r of 160000 and consists of four polypeptides of M r 45000. It shows high substrate specificity, dihydroxyacetone being its only phosphoryl group acceptor and ATP its only phosphoryl group donor; the apparent K m value for dihydroxyacetone was 16 μm and that for ATP 550 μm. It has a pH optimum of 6.5, requires Mg2+ or Ca2+ (the slightly more active ion), and is inhibited by fluoride or ADP but not by dihydroxyacetone phosphate or fructose 1,6-bisphosphate. The isolated enzyme is relatively unstable.
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