Purification, catalytic properties and thermostability of 3-isopropylmalate dehydrogenase from Escherichia coli
- 1 January 1997
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1337 (1) , 105-112
- https://doi.org/10.1016/s0167-4838(96)00157-4
Abstract
No abstract availableKeywords
This publication has 13 references indexed in Scilit:
- Hydrophobic interaction at the subunit interface contributes to the thermostability of 3‐isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilusEuropean Journal of Biochemistry, 1994
- Kinetic analysis on the substrate specificity of 3‐isopropylmalate dehydrogenaseFEBS Letters, 1993
- Structure of isocitrate dehydrogenase with isocitrate, nicotinamide adenine dinucleotide phosphate, and calcium at 2.5-.ANG. resolution: A pseudo-Michaelis ternary complexBiochemistry, 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
- Proteins under extreme physical conditionsFEBS Letters, 1990
- Relationship of protein flexibility to thermostabilityProtein Engineering, Design and Selection, 1987
- Fluctuations in Protein Structure from X-Ray DiffractionAnnual Review of Biophysics and Bioengineering, 1984
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970