PKM2 in cancer cells, such as the human lung cancer cell line H1299, and replacing it with PKM1 was demonstrated to result in a metabolic phenotype change involving decreased glucose uptake and increased oxidative phosphorylation. Further, reprogramming of somatic cells to induced pluripotent stem cells has also been shown to incur metabolic reprogramming; the change from a low glycolytic flux state of somatic cells to a high flux state of rapidly dividing iPSC cells is accompanied by a switch in the isozyme expression of HK and PFK enzymes. An additional layer of flux regulation of glycolysis is exerted by signaling pathways. Through signaling pathways, contrasting glycolysis flux behavior is accomplished without changing the isoforms ; instead the action of signaling pathways alters the kinetic behavior of the target enzyme. Tyrosine kinase signaling has been shown to change the kinetic behavior of PKM2 isoform through modulation of its allosteric regulations. Similarly, signaling events triggered by glucagon in hepatocytes alter the kinetics of the liver isozyme of PK. Protein kinases A/B/C have been shown to affect the kinetics of PFKFB isoforms. The composition of isozymes in glycolysis, through multiple layers of regulation, is pivotal to the flux control and plays a key role in growth control and physiological balance. Over the last four decades, the kinetic behavior of isoforms of individual glycolytic enzymes has been examined in detail. However, a holistic understanding of the effect of different combinations of such isoforms on the flux behavior of the complete glycolysis pathway is yet to be attained. We have taken a systems biology approach to study the flux states of glycolysis pathway. Using a mathematical model that employs mechanistic rate equations for enzyme kinetics, we demonstrate that glycolysis exhibits a classical multiple steady state behavior in terms of its flux with respect to the glucose concentration. The multiplicity of steady states segregate cell metabolism into distinct states: high glycolytic flux states and low glycolytic flux states. Such bistable behavior is an output of complex allosteric regulations which in turn depend on the type of glycolytic isozymes expressed. We show that the presence of the muscle or the liver isozyme of PFK or/and the L, R or M2 isoform of PK is necessary for multistability in glycolytic flux. We substantiated the modeling insights with gene expression data from various tissues as well as experimental data from HeLa cells. Further, we discuss the factors that affect the bistable nature of the glycolysis such as the level and the K/P ratio of enzyme PFKFB. Similar kinds of bistable behavior have been shown to act like a robust switch in many regulatory circuits including oocyte cell maturation, transition between multiple phosphoform stable states in multisite phosphorylation systems, among many others.