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Polyphenol Oxidase

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Food Enzymes

Abstract

Polyphenol oxidase (1,2-benzenediol:oxygen oxidoreductase; EC 1.10.3.1), also known as tyrosinase, phenolase, catechol oxidase, monophenol oxidase, creso-lase, and catecholase, was first discovered in 1856 by Schoenbein (1856) in mushrooms. He noted that something in mushrooms catalyzed the aerobic oxidation of certain compounds in plants. The enzyme is found in many plant tissues (Sherman et al. 1991), in some fungi (especially those that produce brown filaments, Osuga et al. 1994), and in some higher animals, including insects (Sugumaran 1988) and humans (Witkop 1985). In higher plants, the enzyme protects the plant against insects and microorganisms and, when wounded, it forms an impervious scab of melanin against further attack by microorganisms and desiccation (Szent-Györgyi and Vietorisz 1931).

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References

  • Bernan, V.; Filpula, D.; Herber, W.; Bibb, M.; and Katz, E. 1985. The nucleotide sequence of the tyrosinase gene of Streptomyces antibioticus and characterization of the gene product. Gene 37, 101–110.

    Article  CAS  Google Scholar 

  • Bouchilloux, S.; Mcmahill, P.; and Mason, H. S. 1963. The multiple forms of mushroom tyrosinase. Purification and molecular properties of the enzymes. J. Biol. Chem. 238, 1699–1707.

    CAS  Google Scholar 

  • Brooks, D. W., and Dawson, C. R. 1966. Aspects of tyrosinase chemistry. In: The Biochemistry of Copper, J. Peisach, P. Aisen, and W. E. Blumberg, eds., Academic Press, New York, pp. 343–357.

    Google Scholar 

  • Brown, J. M.; Powers, L.; Kincaid, B.; Larrabee, J. A.; and Spiro, T. G. 1980. Structural studies of the hemocyanin active site. 1. Extended X-ray absorption fine structure (EXAFS) analyses. J. Am. Chem. Soc. 102, 4210–4216.

    Article  CAS  Google Scholar 

  • Cary, J. W.; Lax, A. R.; and Flurkey, W. H. 1992. Cloning and characterization of cDNAs coding for Vicia faba polyphenol oxidase. Plant Mol. Biol. 20, 245253.

    Google Scholar 

  • Cleland, W. W. 1963a. The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations. Biochim. Biophys. Acta 67, 104–137.

    Article  CAS  Google Scholar 

  • Cleland, W. W. 1963b. The kinetics of enzyme-catalyzed reactions with two or more substrates or products. II. Inhibition: Nomenclature and theory. Biochim. Biophys. Acta 67, 173–187.

    Article  CAS  Google Scholar 

  • Cleland, W. W. 1963c. The kinetics of enzyme-catalyzed reactions with two or more substrates or products. III. Prediction of initial velocity and inhibition patterns by inspection. Biochim. Biophys. Acta 67, 188–196.

    Article  CAS  Google Scholar 

  • Dawson, C. R., and Mallette, M. F. 1945. Copper proteins. Adv. Prot. Chem. 2, 179–248.

    Article  CAS  Google Scholar 

  • Dietler, C., and Lerch, K. 1982. Reaction inactivation of tyrosinase. In: Oxidases and Related Redox Systems, T. E. King, H. S. Mason, and M. Morrison, eds., Pergamon Press, New York, pp. 305–317.

    Google Scholar 

  • Eickman, N. C.; Solomon, E. I.; Larrabee, J. A.; Spiro, T. G.; and Lerch, K. 1978. Ultraviolet resonance Raman study of oxytyrosinase. Comparison with oxyhemocyanins. J. Am. Chem. Soc. 100, 6529–6531.

    Article  CAS  Google Scholar 

  • Fling, M.; Horowitz, N. H.; and Heinemann, S. F. 1963. The isolation and properties of crystalline tyrosinase from Neurospora. J. Biol. Chem. 238, 2045–2053.

    CAS  Google Scholar 

  • Flurkey, W. H. 1994. Isolation and properties of broad bean polyphenol oxidase. Abstract 91 (AGFD), 208th Am. Chem. Soc. National Meeting, Washington, D.C., August 21–25.

    Google Scholar 

  • Gaykema, W. P. J.; Hol, W. G. J.; Vereuken, J. M.; Soeter, N. M.; Bak, H. J.; and Beintema, J. J. 1984. 3.2 A Structure of the copper-containing, oxygen-carrying protein Panulirus interruptus haemocyanin. Nature 309, 23–29.

    Google Scholar 

  • Golan-Goldmrsh, A.; Osuga, D. T.; Chen, A. O.; and Whitaker, J. R. 1992. Effect of ascorbic acid and copper on proteins and other polymers. In: The Bioorganic Chemistry of Enzymatic Catalysis: An Homage to Myron L. Bender, V. T. D’Souza and J. Feder, eds., CRC Press, Boca Raton, pp. 61–76.

    Google Scholar 

  • Golan-Goldhirsh, A., and Whitaker, J. R. 1984. koat inactivation of mushroom polyphenol oxidase. J. Mol. Catal. 32, 141–147.

    Google Scholar 

  • Gutteridge, S., and Robb, D. 1975. Catecholase activity of Neurospora tyrosinase. Eur. J. Biochem. 54, 107–116.

    Article  CAS  Google Scholar 

  • Himmelwright, R. S.; Eickman, N. C.; Lubien, C. D.; Lerch, K.; and Solomon, E. I. 1980. Chemical and spectral studies of the binuclear copper active site of Neurospora tyrosinase: Comparison to hemocyanin. J. Am. Chem. Soc. 102, 7339–7344.

    Article  CAS  Google Scholar 

  • Huber, M.; Hintermann, G.; and Lerch, K. 1985. Primary structure of tyrosinase from Streptomyces glaucescens. Biochemistry 24, 6038–6044.

    Article  CAS  Google Scholar 

  • Hunt, M. D.; Eannetta, N. T.; Yu, H.; Newman, S. M.; and Steffens, J. C. 1993. cDNA cloning and expression of potato polyphenol oxidase. Plant Mol. Biol. 21, 59–68.

    Google Scholar 

  • Ingraham, L. L. 1959. Polyphenol oxidase at low pH values. In: Pigment Cell Biology, M. Gordon, ed., Academic Press, New York, pp. 609–617.

    Google Scholar 

  • Jolley, R. L., JR.; Ross, D. A.; and Mason, H. S. 1969A. The multiple forms of mushroom tyrosinase. Association-dissociation phenomena. J. Biol. Chem. 244, 1593–1599.

    Google Scholar 

  • Jolley, R. L., Jr.; Nelson, R. M.; and Robb, D. A. 1969B. The multiple forms of mushroom tyrosinase. J. Biol. Chem. 244, 3251–3257.

    Google Scholar 

  • Keilin, D., and Mann, T. 1938. Polyphenol oxidase: Purification, nature and properties. Proc. Royal Soc. Ser B 125, 187–204.

    Article  CAS  Google Scholar 

  • Kitanma, N., and Moro-Oka, Y. 1994. Copper-dioxygen complexes. Inorganic and bioinorganic perspectives. Chem. Rev. 94, 737–757.

    Article  Google Scholar 

  • Korytowski, W.; Sarna, T.; Kalyanaraman, B.; and Sealey, R. C. 1987. Tyrosinase-catalyzed oxidation of dopa and related catechol (amines): A kinetic electron spin resonance investigation using spin-stabilization and spin label oximetry. Biochim. Biophys. Acta 924, 383–392.

    Article  CAS  Google Scholar 

  • Kubowitz, F. 1938. Cleavage and resynthesis of polyphenoloxidase and of hemocyanin. Biochem. Z. 299, 32–57.

    CAS  Google Scholar 

  • Kwon, B. S.; Haq, A. K.; Pomerantz, S. H.; and Halaban, R. 1987. Isolation and sequence of a cDNA clone for human tyrosinase that maps at the mouse c-albino locus. Proc. Natl. Acad. Sci. USA 84, 7473–7477.

    Article  CAS  Google Scholar 

  • Lerch, K. 1978 Amino acid sequence of tyrosinase from Neurospora crassa. Proc. Natl. Acad. Sci. USA 75, 3635–3639.

    Article  CAS  Google Scholar 

  • Lerch, K. 1983. Neurospora tyrosinase: Structural, spectroscopic and catalytic activity. Mol. Cell. Biochem. 52, 125–138.

    CAS  Google Scholar 

  • Lerch, K., and Ettlinger, L. 1972. Purification and characterization of a tyrosinase from Streptomyces glaucescens. Eur. J. Biochem. 31, 427–437.

    Article  CAS  Google Scholar 

  • Lerner, A. B. 1953. Metabolism of phenylalanine and tyrosine. Adv. Enzymol. 14, 73–128.

    CAS  Google Scholar 

  • Macrae, A. R., and Duggleby, R. G. 1968. Substrates and inhibitors of potato tuber phenolase. Phytochemistry 7, 855–861.

    Article  CAS  Google Scholar 

  • Mason, H. S. 1965. Oxidases. Ann. Rev. Biochem. 34, 595–634.

    Article  CAS  Google Scholar 

  • Mason, H. S.; Fowlks, W. B.; and Peterson, E. W. 1955. Oxygen transfer and electron transport by the phenolase complex. J. Am. Chem. Soc. 77, 2914–2915.

    Article  CAS  Google Scholar 

  • Matheis, G., and Whitaker, J. R. 1984. Modification of proteins by polyphenol oxidase and peroxidase and their products. J. Food Biochem. 8, 137–162.

    Article  CAS  Google Scholar 

  • Mayer, A. M.; Harel, E.; and Ben-Shaul, R. 1966. Assay of cathechol oxidase. A critical comparison of methods. Phytochemistry 5, 783–789.

    Article  CAS  Google Scholar 

  • Nelson, J. M., and Dawson, C. R. 1944. Tyrosinase. Adv. Enzymol. 4, 99–152.

    CAS  Google Scholar 

  • Olah, A. F., and Mueller, W. C. 1981. Ultrastructural localization of oxidative and peroxidative activities in a carrot suspension cell culture. Protoplasmia 106, 231–248.

    Article  CAS  Google Scholar 

  • Osuga, D; Van Der Schaaf, A.; and Whitaker, J. R. 1994. Control of polyphenol oxidase activity using a catalytic mechanism. In: Protein Structure-Function Relationships in Foods, R. Y. Yada, R. L. Jackman, and J. L. Smith, eds., Blackie Academic & Professional, Glasgow, Scotland, pp. 62–88.

    Chapter  Google Scholar 

  • Peter, M. G.; Stegmann, H. B.; Dao-Ba, H.; and Scheffler, K. 1985. Detection of semiquinone radicals of N-acyldopamines in aqueous solution. Z. Naturforsch. 40c, 535–538.

    Google Scholar 

  • Quevedo, W. C., Jr. 1971. Genetic regulation of pigmentation in mammals. In: Bio logy of Normal and Abnormal Melanocytes, T. Kawamura and T. B. Fitzpatrick, eds., University Park Press, Baltimore, MD, pp. 99–115.

    Google Scholar 

  • Rivas, N. J., and Whitaker, J. R. 1973. Purification and some properties of two polyphenol oxidases from Bartlett pears. Plant Physiol. 52, 501–507.

    Article  CAS  Google Scholar 

  • Robb, D. A.; Swain, T.; and Mapson, L. W. 1966. Substrates and inhibitors of the activated tyrosinase of broad bean (Vicia faba L.). Photochemistry 5, 665–675.

    Google Scholar 

  • Robinson, S. P., and Dry, I. B. 1992. Broad bean leaf polyphenol oxidase is a 60kilodalton protein susceptible to proteolytic cleavage. Plant Physiol. 99, 317–323.

    Article  CAS  Google Scholar 

  • Rodriquez, M. O., and Flurkey, W. H. 1992. A biochemistry project to study mushroom tyrosinase: Enzyme localization, isoenzymes, and detergent activation. J. Chem. Educ. 69, 767–769.

    Article  CAS  Google Scholar 

  • Saul, S. J., and Sugumaran, M. 1987. Protease mediated prophenoloxidase activation in the hemolymph of the tobacco hornworm, Manduca sexta. Arch. Insect Biochem. Physiol. 5, 1–11.

    Article  CAS  Google Scholar 

  • Saul, S. J., and Sugumaran, M. 1988. Prophenoloxidase activation in the hemolymph of Sarcophaga bullata larvae. Arch. Insect Biochem. Physiol. 7, 91–103.

    Article  CAS  Google Scholar 

  • Schartau, W.; Eyerle, F.; Reisinger, P.; Geisert, H.; Storz, H.; and Linzen, B. 1983. Hemocyanin in spiders. XIX. Complete amino acid sequence of subunit d from Eurypelma californicum hemocyanin, and comparison to chain e. HoppeSeyler’s Z. Physiol. Chem. 364, 1383–1409.

    Article  CAS  Google Scholar 

  • Schneider, H. J.; Drexel, R.; Feldmaier, G.; and Linzen, B. 1983. Hemocyanins in spiders. XVIII. Complete amino-acid sequence of subunit e from Eurypelma californicum hemocyanin. Hoppe-Seyler’s Z. Physiol. Chem. 364, 1357–1381.

    Article  CAS  Google Scholar 

  • Schoenbein, C. F. 1856. On ozone and oronic actions in mushrooms. Phil. Mag. 11, 137–141

    Google Scholar 

  • Shaiiar, T.; Hennig, N.; Gutfinger, T.; Hareven, D.; and Lifschitz, E. 1992. The tomato 66.3-kD polyphenoloxidase gene: Molecular identification and developmental expression. The Plant Cell 4, 135–147.

    Google Scholar 

  • Sherman, T. O.; Vaughn, K. C.; and Duke, S. O. 1991. A limited survey of the phylogenetic distribution of polyphenol oxidase. Phytochemistry 30, 2499–2506.

    Article  CAS  Google Scholar 

  • Shibahara, A.; Tomita, Y.; Sakakura, T.; Nager, C.; Chaudiiuri, B.; and Müller, R. 1986. Cloning and expression of cDNA encoding mouse tyrosinase. Nucl. Acids Res. 14, 2413–2427.

    Article  CAS  Google Scholar 

  • Silvers, W. K. 1979. The Coat Colors of Mice: A Model for Mammalian Gene Action and Interaction. Springer-Verlag, New York.

    Book  Google Scholar 

  • Solomon, E. I.; Baldwin, M. J.; and Lowrey, M. D. 1992. Electronic structures of active sites in copper proteins: Contributions to reactivity. Chem. Rev. 92, 521–542.

    Article  CAS  Google Scholar 

  • Solomon, E. I., and Lowery, M. D. 1993. Electronic structure contributions to function in bioinorganic chemistry. Science 259, 1575–1581.

    Article  CAS  Google Scholar 

  • Sugumaran, M. 1988. Molecular mechanisms for cuticular sclerotization. Adv. Insect Physiol. 21(9), 179–231.

    Google Scholar 

  • Sugumaran, M. 1990. Prophenoloxidase activation and insect immunity. In: Defense Molecules, J. J. Marchalonis and E. L. Reinisch, eds., Wiley-Liss, New York, pp. 47–62.

    Google Scholar 

  • Sugumaran, M. 1994. Regulation of phenoloxidase activity in insects. Abstract 93 (AGFD), 208th Am. Chem. Soc. Nat. Meeting, Washington, D.C., August 21–25.

    Google Scholar 

  • Sugumaran, M.; Hennigan, B.; and O’brien, J. 1987. Tyrosinase catalyzed protein polymerization as an in vitro model for quinone tanning of insect cuticle. Arch. Insect Biochem. Physiol. 6, 9–25.

    Article  CAS  Google Scholar 

  • Szent-Gyrgyi, A., and Vietorisz, K. 1931. Function and significance of polyphenol oxidase from potatoes. Biochem. Z. 233, 236–239.

    Google Scholar 

  • Vaughn, K. C. 1987. Polyphenol oxidase. In: Handbook of Plant Cytochemistry, vol. 1, K. C.Vaughn, ed., CRC Press, Boca Raton, pp. 159–162.

    Google Scholar 

  • Vaughn, K. C., and Duke, S. O. 1981. Tissue localization of polyphenol oxidase in sorghum. Protoplasmia 108, 319–327.

    Article  CAS  Google Scholar 

  • Whitaker, J. R. 1994. Principles of Enzymology for the Food Sciences, Marcel Dekker, New York, pp. 184–192.

    Google Scholar 

  • Wilcox, D. E.; Porras, A. G.; Hwang, Y. T.; Lerch, K.; Winkler, M. E.; and Solomon, E. I. 1985. Substrate analogue binding to the coupled binuclear copper active site in tyrosinase. J. Am. Chem. Soc. 107, 4015–4027.

    Article  CAS  Google Scholar 

  • Witkop, C. J., Jr. 1979. Depigmentations of the general and oral tissues and their genetic foundations. Ala. J. Med. Sci. 16, 331–343.

    Google Scholar 

  • Witkop, C. J., Jr. 1985. Inherited disorders of pigmentation. In: Genodermatoses: Clinics in Dermatology, vol. 2, R. M. Goodman, ed., J. M. Lippincott, Philadelphia, pp. 70–134.

    Google Scholar 

  • Wong, T. C.; Lux, B. S.; and Whitaker, J. R. 1971a. Isolation and characterization of polyphenol oxidases of clingstone peach. Plant Physiol. 48, 19–23.

    Article  CAS  Google Scholar 

  • Wong, T. C.; Lux, B. S.; and Whitaker, J. R. 1971b. Effect of phloroglucinol and resorcinol on the clingstone peach poly-phenol oxidase-catalyzed oxidation of 4-methyl catechol. Plant Physiol. 48, 24–30.

    Article  CAS  Google Scholar 

  • Wood, B. J. B., and Ingraham, L. L. 1965. Labelled tyrosinase from labelled substrate. Nature 205, 291–292.

    Article  CAS  Google Scholar 

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Whitaker, J.R. (1995). Polyphenol Oxidase. In: Food Enzymes. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-2349-6_9

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  • DOI: https://doi.org/10.1007/978-1-4757-2349-6_9

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