ACTIVATION OF RABBIT LIVER FRUCTOSE DIPHOSPHATASE BY COENZYME A AND ACYL CARRIER PROTEIN

Abstract
The catalytic activity of rabbit liver fructose diphosphatase is enhanced more than fourfold by treatment with coenzyme A or acyl carrier protein. Other sulfhydryl compounds, such as glutathione or cysteine, are without effect. Activation is reversed by reduced glutathione or cysteine, indicating that the enzyme and activator are linked by disulfide bridges. The activated enzyme derivative can be formed by a disulfide exchange reaction at alkaline pH or by an oxidation reaction which proceeds at neutral pH. The latter process requires O(2) and Cu(++), and is inhibited by EDTA.