Cofactor-dependent assembly of the flavoenzyme vanillyl-alcohol oxidase.

@article{Tahallah2002CofactordependentAO,
  title={Cofactor-dependent assembly of the flavoenzyme vanillyl-alcohol oxidase.},
  author={Nora Tahallah and Robert van den Heuvel and Willy A. M. van den Berg and Claudia S. Maier and Willem J H van Berkel and Albert J. R. Heck},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 39},
  pages={36425-32}
}
The oligomerization of the flavoprotein vanillyl-alcohol oxidase (VAO) and its site-directed mutant H61T was studied by mass spectrometry. Native VAO has a covalently bound FAD and forms primarily octameric assemblies of 507 kDa. H61T is purified as a FAD-free apoprotein and mainly exists as a dimeric species of 126 kDa. Binding of FAD to apoH61T rapidly… CONTINUE READING