Mutagenesis and Laue structures of enzyme intermediates: isocitrate dehydrogenase
J M Bolduc1, D H Dyer, W G Scott
1Fred Hutchinson Cancer Research Center, Program in Structural Biology, Seattle, WA 98104, USA.
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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