Protein science : a publication of the Protein Society, 5(2), 341-347 (1996-02-01)
The substrate specificity of the NADP-dependent isocitrate dehydrogenase of Escherichia coli was investigated by combining site-directed mutagenesis and utilization of alternative substrates. A comparison of the kinetics of the wild-type enzyme with 2R-malate reveals that the gamma-carboxylate of 2R,3S-isocitrate contributes
European journal of biochemistry, 221(3), 899-903 (1994-05-01)
Isocitrate dehydrogenase (ICDH) from an extreme thermophile, Thermus thermophilus HB8, was overexpressed in Escherichia coli. The enzyme was easily purified to homogeneity by a combination of heat treatment (70 degrees C, 20 min) and column chromatography. The N-terminal sequence of
Metabolism of ethylmalic acids by Pseudomonas aeruginosa.
R Rabin et al.
Biochemistry, 7(1), 377-388 (1968-01-01)
A radioactive assay for malate synthase and other glyoxylate condensing enzymes
Journal of bacteriology, 98(1), 147-151 (1969-04-01)
A mutant strain of Salmonella typhimurium (SL 1634 dml-51) capable of growth on d-malate as sole carbon source was shown to produce d-malic enzyme. This enzyme was absent in the parent wild-type strain which was unable to grow on d-malate.
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