Abstract
SUMMARY: Glucose-6-phosphate isomerase was partially purified from cells of Dictyostelium discoideum in the culmination stage of development. The enzyme had a pH optimum of about 8·5 in Tris/HCl buffer. Activity was not inhibited by p-chloromercuribenzoate or iodoacetate. The enzyme exhibited Michaelis–Menten kinetics and the K m values for glucose 6-phosphate and fructose 6-phosphate were 2 mm and 0·1 mm, respectively. Erythrose 4-phosphate was a strong competitive inhibitor of the enzyme with a K i value of 3·8 μm, whereas 6-phospho-gluconate was less effective with a K i of 0·1 mm.
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