Polyphenol oxidase (PPO; also polyphenol oxidase i, chloroplastic), an enzyme involved in fruit browning, is a tetramer that contains four atoms of copper per molecule.[1]
PPO may accept monophenols and/or o-diphenols as substrates.[2] The enzyme works by catalyzing the o-hydroxylation of monophenol molecules in which the benzene ring contains a single hydroxyl substituent to o-diphenols (phenol molecules containing two hydroxyl substituents at the 1, 2 positions, with no carbon between).[3] It can also further catalyse the oxidation of o-diphenols to produce o-quinones.[4] PPO catalyses the rapid polymerization of o-quinones to produce black, brown or red pigments (polyphenols) that cause 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.[5]
Common foods producing the enzyme include mushrooms (Agaricus bisporus),[6][7] apples (Malus domestica),[8][9] avocados (Persea americana), and lettuce (Lactuca sativa).[10]
^"Polyphenol Oxidase". Worthington Enzyme Manual. Retrieved 13 September 2011.
^McLarin, Mark-Anthony; Leung, Ivanhoe K. H. (2020). "Substrate Specificity of Polyphenol Oxidase". Crit. Rev. Biochem. Mol. Biol.55 (3): 274–308. doi:10.1080/10409238.2020.1768209. PMID 32441137. S2CID 218831573.
^A Sánchez-Ferrer; J N Rodríguez-López; F García-Cánovas; F García-Carmona (1995). "Tyrosinase: A Comprehensive Review of Its Mechanism". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1247 (1): 1–11. doi:10.1016/0167-4838(94)00204-t. PMID 7873577.
^C Eicken; B Krebs; J C Sacchettini (1999). "Catechol Oxidase - Structure and Activity". Current Opinion in Structural Biology. 9 (6): 677–683. doi:10.1016/s0959-440x(99)00029-9. PMID 10607672.
^Mayer AM (November 2006). "Polyphenol oxidases in plants and fungi: going places? A review". Phytochemistry. 67 (21): 2318–31. Bibcode:2006PChem..67.2318M. doi:10.1016/j.phytochem.2006.08.006. PMID 16973188.
^Mauracher SG, Molitor C, Michael C, Kragl M, Rizzi A, Rompel A (March 2014). "High level protein-purification allows the unambiguous polypeptide determination of latent isoform PPO4 of mushroom tyrosinase". Phytochemistry. 99: 14–25. Bibcode:2014PChem..99...14M. doi:10.1016/j.phytochem.2013.12.016. PMC 3969299. PMID 24461779.
^Mauracher SG, Molitor C, Al-Oweini R, Kortz U, Rompel A (September 2014). "Latent and active abPPO4 mushroom tyrosinase cocrystallized with hexatungstotellurate(VI) in a single crystal". Acta Crystallographica. Section D, Biological Crystallography. 70 (Pt 9): 2301–15. doi:10.1107/S1399004714013777. PMC 4157443. PMID 25195745.
^Kampatsikas I, Bijelic A, Pretzler M, Rompel A (August 2017). "Three recombinantly expressed apple tyrosinases suggest the amino acids responsible for mono- versus diphenolase activity in plant polyphenol oxidases". Scientific Reports. 7 (1): 8860. Bibcode:2017NatSR...7.8860K. doi:10.1038/s41598-017-08097-5. PMC 5562730. PMID 28821733.
^Kampatsikas I, Bijelic A, Pretzler M, Rompel A (May 2019). "A Peptide-Induced Self-Cleavage Reaction Initiates the Activation of Tyrosinase". Angewandte Chemie. 58 (22): 7475–7479. doi:10.1002/anie.201901332. PMC 6563526. PMID 30825403.
^Toledo L, Aguirre C (December 2017). "Enzymatic browning in avocado (Persea americana) revisited: History, advances, and future perspectives". Critical Reviews in Food Science and Nutrition. 57 (18): 3860–3872. doi:10.1080/10408398.2016.1175416. PMID 27172067. S2CID 205692816.
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