title: Mutagenesis and Laue structures of enzyme intermediates: isocitrate dehydrogenase.
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.
authors.affiliation: Fred Hutchinson Cancer Research Center, Program in Structural Biology, Seattle, WA 98104, USA.
authors.forename: J M
authors.initials: JM
authors.lastname: Bolduc
authors.forename: D H
authors.initials: DH
authors.lastname: Dyer
authors.forename: W G
authors.initials: WG
authors.lastname: Scott
authors.forename: P
authors.initials: P
authors.lastname: Singer
authors.forename: R M
authors.initials: RM
authors.lastname: Sweet
authors.forename: D E
authors.initials: DE
authors.lastname: Koshland
authors.forename: B L
authors.initials: BL
authors.lastname: Stoddard
mesh_terms: D001665:Binding Sites; D002384:Catalysis; D003196:Computer Graphics; D018360:Crystallography, X-Ray; D007521:Isocitrate Dehydrogenase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D007523:Isocitrates / Q000378:metabolism; D007700:Kinetics; D016297:Mutagenesis, Site-Directed; D009249:NADP / Q000378:metabolism; D011487:Protein Conformation
chemical_list: D007523:Isocitrates; D009249:NADP; C034219:isocitric acid; D007521:Isocitrate Dehydrogenase