Effect of thiohydroxyl compounds on tyrosinase: inactivation and reactivation study.

@article{Park2003EffectOT,
  title={Effect of thiohydroxyl compounds on tyrosinase: inactivation and reactivation study.},
  author={Yong-Doo Park and Su-Jin Lee and Kyung-hee Park and So-Yeon Kim and Myong-Joon Hahn and Jun-Mo Yang},
  journal={Journal of protein chemistry},
  year={2003},
  volume={22 7-8},
  pages={
          613-23
        }
}
An unusual thioether bridge (Cys-His) has been detected at the active site of mushroom tyrosinase, and the effects of thiohydroxyl compounds such as dithiothreitol (DTT) and beta-mercaptoethanol (beta-ME) on Cu2+ at the active site have been elucidated. Treatment with DTT and beta-ME on mushroom tyrosinase completely inactivated 3,4-dihydroxyphenylalanine oxidase activity in a dose-dependent manner. Sequential kinetic studies revealed that DTT and beta-ME caused different mixed-type inhibition… CONTINUE READING
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