A specific enzyme is not necessary for vanadate-induced oxidation of NADH
- 1 July 1980
- journal article
- Published by Springer Nature in Nature
- Vol. 286 (5772) , 516-517
- https://doi.org/10.1038/286516a0
Abstract
It has recently been found that ortho- or metavanadate can effectively block (Na+ + K+)ATPase and that it loses its blocking potency when reduced to the vanadyl (VO2+) ion. The question arose whether vanadate could be involved (reduced) in an NAD-linked enzymatic redox system of the cell. Here we have studied the effect of vanadate on malate dehydrogenase (MDH, EC1.1.1.37) catalysed oxidation of NADH during the formation of malate from oxalacetate in vitro. The MDH reaction was accelerated by vanadate, but we found thatr vanadate does not require the presence of any specific enzyme or substrate to mediate NADH oxidation.Keywords
This publication has 9 references indexed in Scilit:
- Vanadate inhibits (Na+ + K+)ATPase by blocking a conformational change of the unphosphorylated formNature, 1979
- Purified cardiac cell membranes with high (Na+ + K+) ATPase activity contain significant NADH-vanadate reductase activityNature, 1979
- The fate of cytoplasmic vanadium. Implications on (NA,K)-ATPase inhibition.Journal of Biological Chemistry, 1979
- Vanadate inhibits the red cell (Na+, K+) ATPase from the cytoplasmic sideNature, 1978
- Commercial ATP containing traces of vanadate alters the response of (Na+ + K+)ATPase to external potassiumNature, 1978
- Vanadate is a potent (Na,K)-ATPase inhibitor found in ATP derived from muscle.Journal of Biological Chemistry, 1977
- Purification and properties of a highly active ouabain-sensitive Na+, K+-dependent adenosinetriphosphatase from cardiac tissueBiochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1966
- The Ethylenediaminetetraacetate Complexes of Vanadium(V).Acta Chemica Scandinavica, 1957
- An investigation of spontaneous activity at the neuromuscular junction of the ratThe Journal of Physiology, 1956