Channeling of substrates and intermediates in enzyme-catalyzed reactions.

@article{Huang2001ChannelingOS,
  title={Channeling of substrates and intermediates in enzyme-catalyzed reactions.},
  author={X. Huang and H. Holden and F. Raushel},
  journal={Annual review of biochemistry},
  year={2001},
  volume={70},
  pages={
          149-80
        }
}
  • X. Huang, H. Holden, F. Raushel
  • Published 2001
  • Medicine, Chemistry
  • Annual review of biochemistry
  • The three-dimensional structures of tryptophan synthase, carbamoyl phosphate synthetase, glutamine phosphoribosylpyrophosphate amidotransferase, and asparagine synthetase have revealed the relative locations of multiple active sites within these proteins. In all of these polyfunctional enzymes, a product formed from the catalytic reaction at one active site is a substrate for an enzymatic reaction at a distal active site. Reaction intermediates are translocated from one active site to the next… CONTINUE READING
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