Mutagenesis and Laue Structures of Enzyme Intermediates: Isocitrate Dehydrogenase
- 2 June 1995
- journal article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 268 (5215) , 1312-1318
- https://doi.org/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.Keywords
This publication has 21 references indexed in Scilit:
- Crystallographic studies on p21H−ras using the synchrotron Laue method: improvement of crystal quality and monitoring of the GTPase reaction at different time pointsActa Crystallographica Section D-Biological Crystallography, 1994
- Laue diffraction study on the structure of cytochrome c peroxidase compound IStructure, 1994
- Distal pocket polarity in ligand binding to myoglobin: Deoxy and carbonmonoxy forms of a threonine68(E11) mutant investigated by x-ray crystallography and infrared spectroscopyBiochemistry, 1993
- Time‐resolved protein crystallographyProtein Science, 1992
- Art is long and time is fleeting: the current problems and future prospects for time-resolved enzyme crystallographyPhilosophical Transactions A, 1992
- Conventional X-ray diffraction approaches to the study of enzyme mechanism: serine proteinases, aminoacyl-tRNA synthetases and xylose isomerasePhilosophical Transactions A, 1992
- Time-resolved X-ray crystallographic study of the conformational change in Ha-Ras p21 protein on GTP hydrolysisNature, 1990
- The recording and analysis of synchrotron X-radiation Laue diffraction photographsJournal of Applied Crystallography, 1989
- Isotope effect studies of the chemical mechanism of pig heart NADP isocitrate dehydrogenaseBiochemistry, 1988
- Millisecond X-ray diffraction and the first electron density map from Laue photographs of a protein crystalNature, 1987