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Literature summary for 1.1.1.42 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
Search for more literature for 1.1.1.42

Protein Variants

Protein Variants Comment Organism
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

General Stability Organism
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

Organism UniProt Comment Textmining
Aeropyrum pernix Q9YE81
-
-
Aeropyrum pernix DSM 11879 Q9YE81
-
-

Substrates and Products (Substrate)

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

Subunits

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

Temperature Optimum [°C]

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

pH Optimum

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