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Literature summary for 1.1.1.85 extracted from

  • Graczer, E.; Varga, A.; Hajdu, I.; Melnik, B.; Szilagyi, A.; Semisotnov, G.; Zavodszky, P.; Vas, M.
    Rates of unfolding, rather than refolding, determine thermal stabilities of thermophilic, mesophilic, and psychrotrophic 3-isopropylmalate dehydrogenases (2007), Biochemistry, 46, 11536-11549.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
DTT
-
Thermus thermophilus

Cloned(Commentary)

Cloned (Comment) Organism
expressed as His-tagged and non-His-tagged fusion proteins in Escherichia coli Thermus thermophilus

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+
-
Thermus thermophilus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
73300
-
SDS-PAGE Thermus thermophilus

Organism

Organism UniProt Comment Textmining
Thermus thermophilus Q5SIY4
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-isopropylmalate + NAD+
-
Thermus thermophilus 2-ketoisocaproate + NADH + CO2
-
?

Synonyms

Synonyms Comment Organism
3-isopropylmalate dehydrogenase
-
Thermus thermophilus
IPMDH
-
Thermus thermophilus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
time-dependent denaturation-renaturation experiments on IPMDH are presented. Unfolding occurs in a single first-order step with half-times of 1 h. The binding of Mn*IPM (the manganese complex of 3-isopropylmalate) markedly reduces the rates of unfolding. Refolding is a two-step or multistep first-order process involving an inactive intermediate. The restoration of the native structure and reactivation take place with a half-time of a few min Thermus thermophilus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
-
Thermus thermophilus