[Comparative kinetic properties of structure-bound and solubilized L-threonine dehydratase from brewer's yeast].

It has been shown that L-threonine dehydratase (EC 4.2.1.16) of brewer's yeast Saccharomyces carlsbergensis is localized in the mitochondrial fraction. The enzyme is easily solubilized from the mitochondria by changing the pH and ionic strength of the buffer. Some kinetic properties of structure-bound and solubilized L-threonine dehydratase have been compared at pH 6,5. The kinetic plots of the initial rate of the reaction versus initial substrate concentration for both enzymes have a hyperbolic shape; the affinities of both enzymes for the substrate appear to be similar (Km = 20 mM). Both enzymes are inhibited by L-isoleucine, the shape of the kinetic plots being thereby changed into sigmoidal. Solubilization results in a decrease of the mitochondral enzyme sensitivity to the inhibition by L-isoleucine and in an appearance of cooperative interactions between the allosteric sites.