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Literature summary for 1.1.1.85 extracted from

  • Hajdu, I.; Szilagyi, A.; Kardos, J.; Zavodszky, P.
    A link between hinge-bending domain motions and the temperature dependence of catalysis in 3-isopropylmalate dehydrogenase (2009), Biophys. J., 96, 5003-5012.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.1.85

Cloned(Commentary)

Cloned (Comment) Organism
recombinant enzyme expression in Escherichia coli Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information thermodynamic and kinetics analysis, overview Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+
-
 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-isopropylmalate + NAD+
-
 Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
More enzyme structure scheme, domain motions, overview Escherichia coli

Synonyms

Synonyms Comment Organism
IPMDH
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
additional information
-
 reaction temperature dependence, overview Escherichia coli

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
20 40 the van ’t Hoff plot of Km IPM shows sigmoid-like transition within this range Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
 assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Escherichia coli