Mechanism of Inhibition of Glycolysis by Vanadate

  • Julio E. Benabe
  • Luis A. Echegoyen
  • Manuel Martínez-Maldonado
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 208)


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).


Pyruvate Kinase Pyruvate Carboxylase Adenylate Kinase Ethacrynic Acid Phosphoglycerate Mutase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • Julio E. Benabe
    • 2
  • Luis A. Echegoyen
    • 1
  • Manuel Martínez-Maldonado
    • 2
  1. 1.Department of ChemistryUniversity of MiamiMiamiUSA
  2. 2.The Department of MedicineVeterans Administration Hospital and University of Puerto Rico School of MedicineSan JuanUSA

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