Structural and kinetic analyses of the H121A mutant of cholesterol oxidase.

@article{Lim2006StructuralAK,
  title={Structural and kinetic analyses of the H121A mutant of cholesterol oxidase.},
  author={Louis Lim and G. Molla and Nicole Guinn and Sandro Ghisla and Loredano Pollegioni and Alice Vrielink},
  journal={The Biochemical journal},
  year={2006},
  volume={400 1},
  pages={13-22}
}
Cholesterol oxidase is a monomeric flavoenzyme that catalyses the oxidation of cholesterol to cholest-5-en-3-one followed by isomerization to cholest-4-en-3-one. The enzyme from Brevibacterium sterolicum contains the FAD cofactor covalently bound to His121. It was previously demonstrated that the H121A substitution results in a approximately 100 mV decrease in the midpoint redox potential and a approximately 40-fold decrease in turnover number compared to wild-type enzyme [Motteran, Pilone… CONTINUE READING

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