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Enzyme Reactions with Phenolic Compounds1: Effect of O-Methyltransferase on a Natural Substrate of Fruit Polyphenol Oxidase2

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Abstract

PHENOLIC compounds constitute the natural substrates of the enzyme polyphenol oxidase (PPO). Of these, the major substrates of the enzyme in fruits are reported to be o-diphenols (catechols), for example, chlorogenic acid3 (CGA), l-epicatechin4, and dopamine5. If it were possible to modify irreversibly one of the catechol hydroxyl groups in any manner, this would have the following effects of preventing participation in PPO reactions by constituent phenolic compounds: (1) The modified catechols would themselves no longer be substrates of PPO6, (2) the absence of catechols as primers of monophenolase oxidations could, in turn, eliminate the oxidation of constituent monophenols7. Even the first effect alone would eliminate the major proportion of PPO substrates in many plant tissues, as stated here6.

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References

  1. No. 2 in a series. No. 1 appeared in J. Biol. Chem., 237, 2926 (1962).

  2. A preliminary account of this work was presented before the American Society of Biological Chemists in Atlantic City, New Jersey, April 1962.

  3. Weurman, C., and Swain, T., Nature, 172, 678 (1953).

    Article  ADS  CAS  PubMed  Google Scholar 

  4. Siegelman, H. W., Arch. Biochem. Biophys., 56, 97 (1955).

    Article  CAS  PubMed  Google Scholar 

  5. Griffiths, L. A., Nature, 184, 58 (1959).

    Article  ADS  CAS  PubMed  Google Scholar 

  6. Cushing, M. L., J. Amer. Chem. Soc., 70, 1184 (1948).

    Article  CAS  Google Scholar 

  7. Bordner, C. A., and Nelson, J. M., J. Amer. Chem. Sóc., 61, 1507 (1939).

    Article  CAS  Google Scholar 

  8. Axelrod, J., and Tomchick, R., J. Biol. Chem., 233, 702 (1958).

    PubMed  CAS  Google Scholar 

  9. Pellerin, J., and D'Iorio, A., Canad. J. Biochem. Physiol., 36, 491 (1958).

    Article  CAS  PubMed  Google Scholar 

  10. Vorsatz, F., J. prakt. Chem., 145 (n.f.), 265 (1936).

    Article  CAS  Google Scholar 

  11. DeEds, F., Booth, A. N., and Jones, F. T., J. Biol. Chem., 225, 615 (1957).

    PubMed  CAS  Google Scholar 

  12. Moores, R. G., McDermott, D. L., and Wood, T. R., Anal. Chem., 20, 620 (1948).

    Article  CAS  Google Scholar 

  13. De la Haba, G., Jamieson, G. A., Mudd, S. H., and Richards, H. H., J. Amer. Chem. Soc., 81, 3975 (1959).

    Article  CAS  Google Scholar 

  14. Corse, J., Sondheimer, E., and Lundin, R. E., Tetrahedron, 18, 1207 (1962).

    Article  CAS  Google Scholar 

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Authors and Affiliations

  1. Western Regional Research Laboratory, Agricultural Research Service, U.S. Department of Agriculture, Albany, 10, California

    B. J. FINKLE & R. F. NELSON

  2. Biological Sciences Department, California State Polytechnic College, San Luis Obispo, California

    R. F. NELSON

Authors
  1. B. J. FINKLE
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  2. R. F. NELSON
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FINKLE, B., NELSON, R. Enzyme Reactions with Phenolic Compounds1: Effect of O-Methyltransferase on a Natural Substrate of Fruit Polyphenol Oxidase2. Nature 197, 902–903 (1963). https://doi.org/10.1038/197902a0

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