1.1.1.85: 3-isopropylmalate dehydrogenase
This is an abbreviated version!
For detailed information about 3-isopropylmalate dehydrogenase, go to the full flat file.
Word Map on EC 1.1.1.85
Reaction
Synonyms
2-hydroxy-4-methyl-3-carboxyvalerate:NAD+ oxidoreductase, 2R,3S-isopropylmalate:NAD+ oxidoreductase (decaboxylating), 3-IPM dehydrogenase, 3-IPM-DH, 3-isopropylmalate dehydrogenase, 3-isopropylmalateDH, APS IPMDH, beta-IPM dehydrogenase, beta-IPMDH, beta-isopropylmalate dehydrogenase, beta-isopropylmalic enzyme, Bs3-isopropylmalateDH, dehydrogenase, 3-isopropylmalate, IMDH, IPMDH, IPMDH1, IPMDH2, IPMDH3, isopropylmalate dehydrogenase, leuB, NAD-dependent isopropylmalate dehydrogenase, Saci_0600, SbIPMDH, SoIPMDH, threo-Ds-3-isopropylmalate dehydrogenase, Tt-beta-3-isopropylmalateDH, two-domain 3-isopropylmalate dehydrogenase, Ydr417cp
ECTree
1.1.1.85 3-isopropylmalate dehydrogenaseAdvanced search results
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results (General Stability
General Stability on EC 1.1.1.85 - 3-isopropylmalate dehydrogenase
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GENERAL STABILITY 
ORGANISM
UNIPROT
LITERATURE
at pH 7.6, the enzyme from Shewanella oneidensis is slightly more stable against hydrostatic pressure than the enzyme from Shewanella benthica, contrary to the physiological pressures of their normal environments. Pressure unfolding of these enzymes (IPMDHs) follows a two-state unfolding model between a native dimer and two unfolded monomers, and the dimer structure is pressure-tolerant up to 200 MPa
at pH 7.6, the enzyme from Shewanella oneidensis is slightly more stable against hydrostatic pressure than the enzyme from Shewanella benthica, contrary to the physiological pressures of their normal environments. Pressure unfolding of these enzymes (IPMDHs) follows a two-state unfolding model between a native dimer and two unfolded monomers, and the dimer structure is pressure-tolerant up to 200 MPa. The pressure-dependent activity does not originate from structural perturbations such as unfolding or dimer dissociation
dilute solutions, 1 mg/ml or less, precipitate upon thawing
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higher thermal stability of the dimer as compared to monomer. B24-B24' is the major contributor to maintaining subunit-subunit interaction at 64°C
in contrast to 3-isopropylmalate dehydrogenase from other sources, K+ and Na+ are not essential for stability of the Sulfolobus enzyme
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slow inactivation occurs in presence of relatively high concentrations of EDTA, 0.01 M
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