Abstract
The enzyme was prepared in a cell-free state. It had pH optima at 6.9 and 8.1 and a Michaelis constant of 0.0015 [image]. It was inhibited by malonic acid, oxaloacetic acid, Cu ions, borate, oxidized glutathione and Na pyrophosphate. Cytochrome c acted as an efficient H carrier for the enzyme. The reaction product, fumaric acid, was isolated and characterized.