Jan 4, 1997

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

Biochimica Et Biophysica Acta
G WallonT Oshima


3-isopropylmalate dehydrogenase (IPMDH) from Escherichia coli was overexpressed, purified and crystallized. The enzyme was characterized and compared to its thermophilic counterpart from Thermus thermophilus strain HB8. As in the thermophile enzyme, the activity of E. coli IPMDH was dependent on the divalent cations, Mg2+ or Mn2+, with Mn2+ being the preferred cation. Activity was also strongly influenced by KCl: 0.3 M were necessary for the optimal activity. At 40 degrees C the K(m) of E. coli IPMDH was 105 microM for IPM and 321 microM for NAD, the kcat was 69 s-1. The half denaturation temperature was 64 degrees C, which was 20 degrees C lower than that of the thermophile enzyme.

Mentioned in this Paper

Cations, Divalent
Alkalescens-Dispar Group
Alcohol Oxidoreductases
Proteins, Recombinant DNA
Thermus thermophilus extract
Hot Temperature
3-Isopropylmalate dehydrogenase
Substrate Specificity

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