Purification, catalytic properties and thermostability of 3-isopropylmalate dehydrogenase from Escherichia coli.

[1]  T. Oshima,et al.  Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus. , 1994, European journal of biochemistry.

[2]  T. Oshima,et al.  Kinetic analysis on the substrate specificity of 3‐isopropylmalate dehydrogenase , 1993, FEBS letters.

[3]  D. Koshland,et al.  Structure of isocitrate dehydrogenase with isocitrate, nicotinamide adenine dinucleotide phosphate, and calcium at 2.5-A resolution: a pseudo-Michaelis ternary complex. , 1993, Biochemistry.

[4]  Y. Katsube,et al.  Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 A resolution. , 1991, Journal of molecular biology.

[5]  D. Koshland,et al.  Catalytic mechanism of NADP(+)-dependent isocitrate dehydrogenase: implications from the structures of magnesium-isocitrate and NADP+ complexes. , 1991, Biochemistry.

[6]  K. Miyazaki,et al.  Purification, catalytic properties, and thermal stability of threo-Ds-3-isopropylmalate dehydrogenase coded by leuB gene from an extreme thermophile, Thermus thermophilus strain HB8. , 1990, Journal of biochemistry.

[7]  M. Inouye,et al.  Low copy number plasmids for regulated low-level expression of cloned genes in Escherichia coli with blue/white insert screening capability. , 1990, Nucleic acids research.

[8]  R. Jaenicke,et al.  Proteins under extreme physical conditions , 1990, FEBS letters.

[9]  M Vihinen,et al.  Relationship of protein flexibility to thermostability. , 1987, Protein engineering.

[10]  M. M. Bradford.  A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. , 1976, Analytical biochemistry.

[11]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.