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Glycerol kinase of Escherichia coli has been purified and crystallized. It has a molecular weight of ∼3 x 105. The enzyme phosphorylates glycerol exclusively to l-α-glycerophosphate. It also catalyzes the phosphorylation of dihydroxyacetone and l-glyceraldehyde but with values of Km much higher than that for glycerol. d-Glyceraldehyde has a catalytic effect in promoting the conversion of adenosine triphosphate to adenosine diphosphate and Pi in the presence of the enzyme. Among the nucleoside triphosphates tested, only adenosine triphosphate was active as the phosphoryl group donor. Mn++ substitutes for Mg++, although with less activity at equal molar concentration.
Hayashi et al. (1967) studied this question.