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Literature summary extracted from

  • Karlström, M.; Chiaraluce, R.; Giangiacomo, L.; Steen, I.H.; Birkeland, N.K.; Ladenstein, R.; Consalvi, V.
    Thermodynamic and kinetic stability of a large multi-domain enzyme from the hyperthermophile Aeropyrum pernix (2010), Extremophiles, 14, 213-223.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.42 R211M disruption of the seven-membered inter-domain ionic network. In wild-type enzyme the unfolding and folding transitions occurrs at slightly different denaturant concentrations even after prolonged equilibration time. The difference between the folding and the unfolding profiles is decreased in the mutant R211M Aeropyrum pernix

General Stability

EC Number General Stability Organism
1.1.1.42 the inter-domain ionic network might be responsible for additional stabilization through a significant kinetic barrier in the unfolding pathway that can explain the larger difference observed between the folding and unfolding transitions of the wild type comparted to the mutant enzyme R211M Aeropyrum pernix

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.42 Aeropyrum pernix Q9YE81
-
-
1.1.1.42 Aeropyrum pernix DSM 11879 Q9YE81
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.42 isocitrate + NADP+
-
Aeropyrum pernix 2-oxoglutarate + CO2 + NADPH + H+
-
?
1.1.1.42 isocitrate + NADP+
-
Aeropyrum pernix DSM 11879 2-oxoglutarate + CO2 + NADPH + H+
-
?

Subunits

EC Number Subunits Comment Organism
1.1.1.42 dimer dissociation from dimer to monomer at pH 3.0 Aeropyrum pernix
1.1.1.42 monomer dissociation from dimer to monomer at pH 3.0 Aeropyrum pernix

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.42 50
-
assay at Aeropyrum pernix

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.42 7.5
-
assay at Aeropyrum pernix