AbstractA graphical method to reveal the so-called ‘critical fragments’ in schemes of biochemical systems is considered. These fragments produce multiple steady states or self-oscillations in systems. As an example, the bifunctional enzyme, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, regulated by glucagon through enzyme phosphorylation, is discussed. It is shown that this enzyme may act as a metabolic switching mechanism in discontinuous or oscillatory regimes, depending on the specific structure of its kinetic scheme. The boundaries of concentrational and parameter domains for these critical phenomena are also predicted
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