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Literature summary for 1.1.1.286 extracted from

  • Miyazaki, K.
    Bifunctional isocitrate-homoisocitrate dehydrogenase: a missing link in the evolution of beta-decarboxylating dehydrogenase (2005), Biochem. Biophys. Res. Commun., 331, 341-346.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Pyrococcus horikoshii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0164
-
isocitrate 70┬░C, pH 7.8 Pyrococcus horikoshii
0.0183
-
homoisocitrate 70┬░C, pH 7.8 Pyrococcus horikoshii
0.0771
-
NAD+ 70┬░C, pH 7.8 Pyrococcus horikoshii

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii
-
expression in Escherichia coli
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme expressed in Escherichia coli, purification of inclusion bodies requires N-laurylsarcosine Pyrococcus horikoshii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
homoisocitrate + NAD+
-
Pyrococcus horikoshii ? + NADH
-
?
isocitrate + NAD+ about 20times more efficient than homoisocitrate, NAD+ is preferred over NADP+ Pyrococcus horikoshii 2-oxoglutarate + CO2 + NADH + H+
-
?
isocitrate + NADP+ NAD+ is preferred over NADP+ Pyrococcus horikoshii 2-oxoglutarate + CO2 + NADPH + H+
-
?
additional information no substrate: 3-isopropylmalate Pyrococcus horikoshii ?
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
13.7
-
homoisocitrate 70┬░C, pH 7.8 Pyrococcus horikoshii
14.8
-
isocitrate 70┬░C, pH 7.8 Pyrococcus horikoshii
21.8
-
NAD+ 70┬░C, pH 7.8 Pyrococcus horikoshii