1887

Abstract

Glucose-6-phosphate isomerase was partially purified from cells of 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 -chloromercuribenzoate or iodoacetate. The enzyme exhibited MichaelisMenten kinetics and the values for glucose 6-phosphate and fructose 6-phosphate were 2 m and 0·1 m, respectively. Erythrose 4-phosphate was a strong competitive inhibitor of the enzyme with a value of 3·8 μ, whereas 6-phospho-gluconate was less effective with a of 0·1 mm.

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/content/journal/micro/10.1099/00221287-124-2-403
1981-06-01
2021-05-07
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