| Polyphenol oxidase |
| Identifiers |
| EC number |
1.14.18.1 |
| CAS number |
9002-10-2 |
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KEGG entry |
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metabolic pathway |
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RCSB PDB PDBe PDBsum |
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Main article: Tyrosinase
Main article: Catechol oxidase
Polyphenol oxidase (PPO or monophenol monooxygenase or Polyphenol oxidase I, chloroplastic) is a tetramer that contains four atoms of copper per molecule, and binding sites for two aromatic compounds and oxygen.[1] The enzyme catalyses the o-hydroxylation of monophenols (phenol molecules in which the benzene ring contains a single hydroxyl substituent) to o-diphenols (phenol molecules containing two hydroxyl substituents). They can also further catalyse the oxidation of o-diphenols to produce o-quinones. It is the rapid polymerization of o-quinones to produce black, brown or red pigments (polyphenols) that is the cause of fruit browning. The amino acid tyrosine contains a single phenolic ring that may be oxidised by the action of PPOs to form o-quinone. Hence, PPOs may also be referred to as tyrosinases.[2]
Common examples of organisms producing the enzyme are Agaricus bisporus, Malus domestica, Lactuca sativa.
Polyphenol oxidase is listed as a morpheein, a protein that can form two or more different homo-oligomers (morpheein forms), but must come apart and change shape to convert between forms. It exists as monomer, trimer, tetramer, octamer, dodecamer.[3][4] Evidences for this are multiple (protein moonlighting functions,[5] Substrate binding/turnover impacts multimerization,[6] Different assemblies have different activities,[7] Kinetic hysteresis[6]).
In plants, PPO is a plastidic enzyme with unclear synthesis and function. In functional chloroplasts, it may be involved in some aspect of oxygen chemistry like mediation of pseudocyclic photophosphorylation.[8]
Enzyme nomenclature differentiates between monophenol oxidase enzymes (tyrosinases) and o-diphenol:oxygen oxidoreductase enzymes (catechol oxidases). Therefore, please refer to the tyrosinase and catechol oxidase articles for more information on polyphenol oxidase enzymes.
A mixture of monophenol oxidase and catechol oxidase enzymes is present in nearly all plant tissues, and can also be found in bacteria, animals, and fungi. In insects, cuticular polyphenol oxidases are present[9] and their products are responsible for desiccation tolerance.
In fact, browning by PPO is not always an undesirable reaction; the familiar brown color of tea (especially black tea) and cocoa[10] is developed by PPO enzymatic browning during product processing.
Grape reaction product (2-S glutathionyl caftaric acid) is an oxidation compound produced by action of PPO on caftaric acid and found in wine. This compound production is responsible for the lower level of browning in certain white wines.
Arctic Apples are a suite of trademarked apples that contain a nonbrowning trait. Specifically, gene silencing is used to turn down the expression of polyphenol oxidase (PPO), thus preventing the fruit from browning. They are therefore genetically modified food.
Contents
- 1 Inhibitors
- 2 Related enzymes
- 3 See also
- 4 References
Inhibitors
There are two types of inhibitor of polyphenol oxidase. Those competitive to oxygen in the copper site of the enzyme and those competitive to phenolics. Tentoxin has also been used in recent research to eliminate the polyphenol oxidase activity from seedlings of higher plants.[11] Tropolone is a grape polyphenol oxidase inhibitor.[12] Another inhibitor of this enzyme is potassium pyrosulphite (K2S2O5).[13] Banana root PPO is strongly inhibited by dithiothreitol and sodium metabisulfite.[14]
Potassium dithionite (or potassium hydrosulfite) is also an inhibitor of the polyphenol oxidase.
Related enzymes
Prophenoloxidase is a modified form of the complement response found in some invertebrates, including insects, crabs and worms.[15]
Hemocyanin is homologous to the phenol oxidases (e.g. tyrosinase) since both enzymes sharing type 3 Cu active site coordination. Hemocyanin also exhibits phenol oxidase activity, but with slowed kinetics from greater steric bulk at the active site. Partial denaturation actually improves hemocyanin’s phenol oxidase activity by providing greater access to the active site.[16]
Aureusidin synthase is homologous to plant polyphenol oxidase, but contains certain significant modifications.
See also
References
- ^ http://www.worthington-biochem.com/TY/default.html, Polyphenol Oxidase - Worthington Enzyme Manual. Accessed 13 September 2011
- ^ Mayer, AM (November 2006). "Polyphenol oxidases in plants and fungi: Going places? A review". Phytochemistry 67 (21): 2318–2331. doi:10.1016/j.phytochem.2006.08.006. PMID 16973188.
- ^ Jolley Jr, RL; Mason, HS (1965). "The Multiple Forms of Mushroom Tyrosinase. Interconversion". The Journal of Biological Chemistry 240: PC1489–91. PMID 14284774.
- ^ Jolley Jr, RL; Robb, DA; Mason, HS (1969). "The multiple forms of mushroom tyrosinase. Association-dissociation phenomena". The Journal of Biological Chemistry 244 (6): 1593–9. PMID 4975157.
- ^ Mallette, MF; Dawson, CR (1949). "On the nature of highly purified mushroom tyrosinase preparations". Archives of biochemistry 23 (1): 29–44. PMID 18135760.
- ^ a b Chazarra, Soledad; Garcı́a-Carmona, Francisco; Cabanes, Juana (2001). "Hysteresis and Positive Cooperativity of Iceberg Lettuce Polyphenol Oxidase". Biochemical and Biophysical Research Communications 289 (3): 769–75. doi:10.1006/bbrc.2001.6014. PMID 11726215.
- ^ Harel, E.; Mayer, A.M. (1968). "Interconversion of sub-units of catechol oxidase from apple chloroplasts". Phytochemistry 7 (2): 199. doi:10.1016/S0031-9422(00)86315-3.
- ^ Function of polyphenol oxidase in higher plants. Kevin C. Vaughn and Stephen O. Duke, Physiologia Plantarum, January 1984, Volume 60, Issue 1, pages 106–112, doi:10.1111/j.1399-3054.1984.tb04258.x
- ^ Sugumaran M, Lipke H (May 1983). "Quinone methide formation from 4-alkylcatechols: a novel reaction catalyzed by cuticular polyphenol oxidase". FEBS Letters 155 (1): 65–68. doi:10.1016/0014-5793(83)80210-5.
- ^ Quesnel V.C., Jugmohunsingh K. (May 2006). "Browning reaction in drying caco". Journal of the Science of Food and Agriculture 21 (10): 537–541. doi:10.1002/jsfa.2740211011.
- ^ Duke SO, Vaughn KC (April 1982). "Lack of involvement of polyphenol oxidase in ortho-hydroxylation of phenolic compounds in mung bean seedlings". Physiologia Plantarum 54 (4): 381–385. doi:10.1111/j.1399-3054.1982.tb00696.x.
- ^ Time-dependent inhibition of grape polyphenol oxidase by tropolone. Edelmira Valero, Manuela Garcia-Moreno, Ramon Varon and Francisco Garcia-Carmona, J. Agric. Food Chem., 1991, 39 (6), pp 1043–1046, doi:10.1021/jf00006a007
- ^ Del Signore A, Romeoa F, Giaccio M (May 1997). "Content of phenolic substances in basidiomycetes". Mycological Research 101 (5): 552–556. doi:10.1017/S0953756296003206.
- ^ Extraction and partial characterization of polyphenol oxidase from banana (Musa acuminata Grande naine) roots. Wuyts N, De Waele D and Swennen R, Plant Physiol Biochem., May-Jun 2006, 44(5-6), pages 308-314, PubMed
- ^ Immunity and the Invertebrates Beck, Gregory and Habicht, Gail S, Scientific American, November 1996, pages 60-66
- ^ Decker H, Tuczek F (August 2000). "Tyrosinase/catecholoxidase activity of hemocyanins: structural basis and molecular mechanism". Trends Biochem. Sci. 25 (8): 392–7. doi:10.1016/S0968-0004(00)01602-9. PMID 10916160.
