Abstract
Vanadate is a well known inhibitor of the Na+, K+-ATPase (1,2). In addition to the effects on the sodium pump, vanadium compounds have been shown to inhibit acid phosphatase, alkaline phosphatase and adenylate kinase (3,4) as well as several of the enzymes in the glycolytic pathway (5), including glyceraldehyde-3-posphate dehydrogenase (6) phosphoglucomutase and phosphoglyceromutase (7–10). Since vanadate can adopt a stable trigonal bipyramidal structure which resembles phosphate, it could inhibit enzyme activity by replacing phosphate as a substrate in transfer or release reactions and lead to the formation of unstable analogues (5–7). This hypothesis, nevertheless, may not completely explain the inhibitory effect of vanadate on glycolytic enzymes. An alternative mechanism may be the influx of extracellular calcium into cells by inhibition of Na+, K+-ATPase (11,12) or Ca++-ATPase (11, 12). This would decrease the cell requirements for ATP (thus, decreasing the rate of glycolysis) by reduction in the activity of the ATPases or inhibition of phophofructokinase, pyruvate kinase or pyruvate carboxylase in the glycolytic pathway (13, 14).
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Benabe, J.E., Echegoyen, L.A., Martínez-Maldonado, M. (1986). Mechanism of Inhibition of Glycolysis by Vanadate. In: Massry, S.G., Olmer, M., Ritz, E. (eds) Phosphate and Mineral Homeostasis. Advances in Experimental Medicine and Biology, vol 208. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5206-8_64
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DOI: https://doi.org/10.1007/978-1-4684-5206-8_64
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