Functional interaction of diphenols with polyphenol oxidase. Molecular determinants of substrate/inhibitor specificity.

@article{Kanade2007FunctionalIO,
  title={Functional interaction of diphenols with polyphenol oxidase. Molecular determinants of substrate/inhibitor specificity.},
  author={Santosh R. Kanade and Venkatramana Laxminarayana Suhas and Nagasuma Chandra and Lalitha Ramakrishna Gowda},
  journal={The FEBS journal},
  year={2007},
  volume={274 16},
  pages={4177-87}
}
Polyphenol oxidase (PPO) catalyzes the oxidation of o-diphenols to their respective quinones. The quinones autopolymerize to form dark pigments, an undesired effect. PPO is therefore the target for the development of antibrowning and antimelanization agents. A series of phenolic compounds experimentally evaluated for their binding affinity and inhibition constants were computationally docked to the active site of catechol oxidase. Docking studies suggested two distinct modes of binding… CONTINUE READING

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