RT Journal Article SR Electronic(1) A1 Thomas, David A.YR 1981 T1 Partial Purification and Characterization of Glucose-6-phosphate Isomerase from Dictyostelium discoideum JF Microbiology, VO 124 IS 2 SP 403 OP 407 DO https://doi.org/10.1099/00221287-124-2-403 PB Microbiology Society, SN 1465-2080, AB 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., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-124-2-403