Research Articles

Mutagenesis and Laue structures of enzyme intermediates: isocitrate dehydrogenase

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Science  02 Jun 1995:
Vol. 268, Issue 5215, pp. 1312-1318
DOI: 10.1126/science.7761851

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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