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Literature summary for 1.1.1.42 extracted from

  • Madern, D.; Camacho, M.; Rodríguez-Arnedo, A.; Bonete, M.J.; Zaccai, G.
    Salt-dependent studies of NADP-dependent isocitrate dehydrogenase from the halophilic archaeon Haloferax volcanii (2004), Extremophiles, 8, 377-384.
    View publication on PubMed

General Stability

General Stability Organism
enzyme stability is mainly sensitive to cations and very little or not sensitive to anions. Divalent cations induce a strong shift of the active/inactive transition towards low salt concentration. Deactivation due to incubation of the enzyme at low NaCl concentrations is related to irreversible dissociation of the active dimeric species towards a monomer, which can be described as an extended inactive monomeric species Haloferax volcanii
with a residual amount of secondary structure Haloferax volcanii

Organism

Organism UniProt Comment Textmining
Haloferax volcanii Q8X277
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Subunits

Subunits Comment Organism
dimer the enzyme is a dimer at high salt concentration. Deactivation due to incubation of the enzyme at low NaCl concentrations is related to irreversible dissociation of the active dimeric species towards a monomer Haloferax volcanii

Synonyms

Synonyms Comment Organism
NADP-dependent isocitrate dehydrogenase
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Haloferax volcanii