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Enolase and Fluorophosphate

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An Erratum to this article was published on 01 July 1964

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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

  1. Warburg, O., and Christian, W., Biochem. Z., 310, 385 (1941).

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  2. Miller, G. W., Plant Physiol., 33, 199 (1958).

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  3. Malmström, B. G., in The Enzymes, edit. by Boyer, P. D., Lardy, H., and Myrback, K., 5, Chap. 29, 471 (1961).

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  4. Tietz, A., and Ochos, S., Arch. Biochim. Biophys., 78, 477 (1958).

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Author notes

  1. L. R. MURRAY

    Present address: Animal Industry Branch, Alice Springs, Northern Territory, Australia

Authors and Affiliations

  1. Department of Biochemistry, University of Cambridge,

    RUDOLPH A. PETERS, M. SHORTHOUSE & L. R. MURRAY

Authors
  1. RUDOLPH A. PETERS
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  2. M. SHORTHOUSE
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  3. L. R. MURRAY
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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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