Pyruvate kinase also serves as a regulatory enzyme for gluconeogenesis, a biochemical pathway in which the liver generates glucose from pyruvate and other substrates. When pyruvate kinase is inhibited by phosphorylation (which occurs in the fasting state, via glucagon), phosphoenolpyruvate is prevented from being converted to pyruvate. Instead, it is converted to glucose in a series of gluconeogenesis reactions that are mostly (but not exactly) the reverse sequence of glycolysis.
The glucose thus produced is expelled from the liver, providing energy for vital tissues in the fasting state.