SUMMARY: Dihydroxyacetone kinase (ATP: dihydroxyacetone phosphotransferase) from has been purified and characterized. It has an of 160000 and consists of four polypeptides of 45000. It shows high substrate specificity, dihydroxyacetone being its only phosphoryl group acceptor and ATP its only phosphoryl group donor; the apparent value for dihydroxyacetone was 16 μ and that for ATP 550 μ. It has a pH optimum of 6.5, requires Mg or Ca (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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