Reference: Bolduc JM, et al. (1995) Mutagenesis and Laue structures of enzyme intermediates: isocitrate dehydrogenase. Science 268(5215):1312-8

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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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Journal Article | Research Support, U.S. Gov't, Non-P.H.S. | Research Support, U.S. Gov't, P.H.S.
Authors
Bolduc JM, Dyer DH, Scott WG, Singer P, Sweet RM, Koshland DE, Stoddard BL
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