Engineering secondary structure to invert coenzyme specificity in isopropylmalate dehydrogenase
- 1 January 1997
- book chapter
- Published by Elsevier in Techniques in Protein Chemistry
Abstract
No abstract availableThis publication has 12 references indexed in Scilit:
- A highly active decarboxylating dehydrogenase with rationally inverted coenzyme specificity.Proceedings of the National Academy of Sciences, 1995
- The role of glutamate 87 in the kinetic mechanism ofThermus thermophilusisopropylmalate dehydrogenaseProtein Science, 1995
- Mutagenesis and Laue Structures of Enzyme Intermediates: Isocitrate DehydrogenaseScience, 1995
- Structure of 3–isopropylmalate dehydrogenase in complex with NAD+: ligand–induced loop closing and mechanism for cofactor specificityStructure, 1994
- Co-enzyme specificity of 3-isopropylmalate dehydrogenase from Thermits thermophilus HB8Protein Engineering, Design and Selection, 1994
- Kinetic mechanism of Escherichia coli isocitrate dehydrogenaseBiochemistry, 1993
- Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 Å resolutionJournal of Molecular Biology, 1991
- Catalytic mechanism of NADP+-dependent isocitrate dehydrogenase: implications from the structures of magnesium-isocitrate and NADP+ complexesBiochemistry, 1991
- Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase.Proceedings of the National Academy of Sciences, 1989
- Chemical and biological evolution of a nucleotide-binding proteinNature, 1974