Substrate specificity of polyphenol oxidase

  title={Substrate specificity of polyphenol oxidase},
  author={Mark-Anthony McLarin and I. K. H. Leung},
  journal={Critical Reviews in Biochemistry and Molecular Biology},
  pages={274 - 308}
  • Mark-Anthony McLarin, I. K. H. Leung
  • Published 2020
  • Chemistry, Medicine
  • Critical Reviews in Biochemistry and Molecular Biology
  • Abstract The ubiquitous type-3 copper enzyme polyphenol oxidase (PPO) has found itself the subject of profound inhibitor research due to its role in fruit and vegetable browning and mammalian pigmentation. The enzyme itself has also been applied in the fields of bioremediation, biocatalysis and biosensing. However, the nature of PPO substrate specificity has remained elusive despite years of study. Numerous theories have been proposed to account for the difference in tyrosinase and catechol… CONTINUE READING
    1 Citations

    Topics from this paper.


    Polyphenol oxidases in plants and fungi: going places? A review.
    • 609
    • Highly Influential
    • PDF
    Crystal structure of a plant catechol oxidase containing a dicopper center
    • 632
    • Highly Influential
    • PDF
    Determination of tyrosinase substrate-binding modes reveals mechanistic differences between type-3 copper proteins.
    • 85
    • Highly Influential
    • PDF
    Unraveling Substrate Specificity and Catalytic Promiscuity of Aspergillus oryzae Catechol Oxidase
    • 3
    Structure–function correlations in tyrosinases
    • 82
    • Highly Influential
    • PDF
    Tyrosinase versus Catechol Oxidase: One Asparagine Makes the Difference.
    • 63
    • Highly Influential
    Crystal structure of Manduca sexta prophenoloxidase provides insights into the mechanism of type 3 copper enzymes
    • 136
    • PDF