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Mutagenesis and Laue structures of enzyme intermediates: isocitrate dehydrogenase.

  • Author(s): Bolduc, JM
  • Dyer, DH
  • Scott, WG
  • Singer, P
  • Sweet, RM
  • Koshland, DE
  • Stoddard, BL
  • et al.
Abstract

Site-directed mutagenesis and Laue diffraction data to 2.5 A resolution were used to solve the structures of two sequential intermediates formed during the catalytic actions of isocitrate dehydrogenase. Both intermediates are distinct from the enzyme-substrate and enzyme-product complexes. Mutation of key catalytic residues changed the rate determining steps so that protein and substrate intermediates within the overall reaction pathway could be visualized.

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