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Literature summary for 1.1.1.87 extracted from

  • Lin, Y.; West, A.H.; Cook, P.F.
    Potassium is an activator of homoisocitrate dehydrogenase from Saccharomyces cerevisiae (2008), Biochemistry, 47, 10809-10815.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.1.87

Inhibitors

Inhibitors Comment Organism Structure
acetate slight inhibition Saccharomyces cerevisiae
Cl-
-
 Saccharomyces cerevisiae
additional information product and dead-end inhibition studies in the absence of K+ Saccharomyces cerevisiae
NAD+ substrate inhibition at high concentrations and in absence of K+, kinetics, overview Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information substitution of potassium acetate for KCl changes the kinetic mechanism of HIcDH from a steady state random to a fully ordered mechanism with the binding of Mg-HIc followed by K+ and NAD+, increase in the affinity of enzyme for Mg-HIc as a result of elimination of the inhibitory effect of Cl-, kinetic analysis, overview Saccharomyces cerevisiae
0.3
-
 NAD+ pH 8.0, 25°C, in presence of K+ Saccharomyces cerevisiae
9
-
 NAD+ pH 8.0, 25°C, in absence of K+ Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
K+ activates Saccharomyces cerevisiae
Mg2+ activates, increase in the affinity of enzyme for Mg-HIc as a result of elimination of the inhibitory effect of Cl- Saccharomyces cerevisiae
additional information selectivity of the activator site for monovalent ions, K+ is the best activator, and NH4+ and Rb+ are also activators of the reaction, while Cs+, Li+, and Na+ are not, overview. Substitution of potassium acetate for KCl changes the kinetic mechanism of HIcDH from a steady state random to a fully ordered mechanism with the binding of Mg-HIc followed by K+ and NAD+ Saccharomyces cerevisiae
NH4+ activates Saccharomyces cerevisiae
Rb+ activates Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ Saccharomyces cerevisiae
-
 2-oxoadipate + NADH + H+ + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
-
 Saccharomyces cerevisiae 2-oxoadipate + NADH + H+ + CO2
-
 ?
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ substitution of potassium acetate for KCl changes the kinetic mechanism of HIcDH from a steady state random to a fully ordered mechanism with the binding of Mg-HIc followed by K+ and NAD+ Saccharomyces cerevisiae 2-oxoadipate + NADH + H+ + CO2
-
 ?
isocitrate + NAD+ low activity Saccharomyces cerevisiae ? + NADH + H+
-
 ?

Synonyms

Synonyms Comment Organism
HIc
-
 Saccharomyces cerevisiae
HIc dehydrogenase
-
 Saccharomyces cerevisiae
HICDH
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Saccharomyces cerevisiae

pH Range

pH Minimum pH Maximum Comment Organism
additional information
-
 pH-rate profile in the absence of K+, overview Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Saccharomyces cerevisiae

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
77
-
 NAD+ pH 8.0, 25°C, in absence of KOAc Saccharomyces cerevisiae