Abstract
IT is commonly believed that the remarkable inhibition of the enzyme enolase by fluoride plus phosphate is due to the formation of fluorophosphate, a belief which is based on the hypothesis advanced by Warburg and Christian1 to explain their interesting facts. This enzyme, now known as phosphopyruvate hydrolase, is numbered 4.2.1.11 by the Enzyme Commission and catalyses the step in glycolysis D-2 -phosphoglycerate ←phospho-enolpyruvate + water.
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Change history
01 July 1964
In the communication entitled "Enolase and Fluorophosphate" by Sir Rudolph Peters, M. Short-house and L. R. Murray, which appeared on p. 1331 of the June 27 issue of Nature, for hydrolase in line 6 read hydratase; Table 1, lines 7 and 8, for FPO3 read FPO2= ; line 2 of the final paragraph, for K2PO3renad K2F.
References
Warburg, O., and Christian, W., Biochem. Z., 310, 385 (1941).
Miller, G. W., Plant Physiol., 33, 199 (1958).
Malmström, B. G., in The Enzymes, edit. by Boyer, P. D., Lardy, H., and Myrback, K., 5, Chap. 29, 471 (1961).
Tietz, A., and Ochos, S., Arch. Biochim. Biophys., 78, 477 (1958).
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PETERS, R., SHORTHOUSE, M. & MURRAY, L. Enolase and Fluorophosphate. Nature 202, 1331–1332 (1964). https://doi.org/10.1038/2021331b0
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DOI: https://doi.org/10.1038/2021331b0
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