%0 Journal Article %A Thomas, David A. %T Partial Purification and Characterization of Glucose-6-phosphate Isomerase from Dictyostelium discoideum %D 1981 %J Microbiology, %V 124 %N 2 %P 403-407 %@ 1465-2080 %R https://doi.org/10.1099/00221287-124-2-403 %I Microbiology Society, %X 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 MichaelisMenten 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. %U https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-124-2-403