Modification of catalytic properties of chicken liver fructose 1,6-bisphosphatase by allicin.

The activity of chicken liver fructose 1,6-bisphosphatase increases dramatically after incubation with allicin, a major biologically active compound produced by garlic. Activation is more pronounced when the enzyme is assayed with Mn2+ than Mg2+. Maximum activation is accompanied by the disappearance of 4 highly reactive sulfhydryl groups per molecule of enzyme. This modification also leads to loss of activation by K+, and reduced sensitivity to inhibition by AMP, fructose 2,6-bisphosphate, and high concentration of fructose 1,6-bisphosphate. All the altered properties induced by allicin can be reversed by dithiothreitol or tris(2-carboxyethyl)phosphine, the latter being much more effective.