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Science 2 June 1995:
Vol. 268. no. 5215, pp. 1312 - 1318
DOI: 10.1126/science.7761851
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Articles

Science, Vol 268, Issue 5215, 1312-1318
Copyright © 1995 by American Association for the Advancement of Science

articles

Mutagenesis and Laue structures of enzyme intermediates: isocitrate dehydrogenase

JM Bolduc, DH Dyer, WG Scott, P Singer, RM Sweet, DE Koshland Jr, and BL Stoddard

Fred Hutchinson Cancer Research Center, Program in Structural Biology, Seattle, WA 98104, USA.

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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