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Literature summary 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

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.87 acetate slight inhibition Saccharomyces cerevisiae
1.1.1.87 Cl-
-
 Saccharomyces cerevisiae
1.1.1.87 additional information product and dead-end inhibition studies in the absence of K+ Saccharomyces cerevisiae
1.1.1.87 NAD+ substrate inhibition at high concentrations and in absence of K+, kinetics, overview Saccharomyces cerevisiae
1.1.1.286 3-carboxypropylidenemalate
-
 Saccharomyces cerevisiae
1.1.1.286 Cl-
-
 Saccharomyces cerevisiae
1.1.1.286 NADH product inhibitor Saccharomyces cerevisiae
1.1.1.286 potassium acetate
-
 Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.87 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
1.1.1.87 0.3
-
 NAD+ pH 8.0, 25°C, in presence of K+ Saccharomyces cerevisiae
1.1.1.87 9
-
 NAD+ pH 8.0, 25°C, in absence of K+ Saccharomyces cerevisiae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.87 K+ activates Saccharomyces cerevisiae
1.1.1.87 Mg2+ activates, increase in the affinity of enzyme for Mg-HIc as a result of elimination of the inhibitory effect of Cl- Saccharomyces cerevisiae
1.1.1.87 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
1.1.1.87 NH4+ activates Saccharomyces cerevisiae
1.1.1.87 Rb+ activates Saccharomyces cerevisiae
1.1.1.286 K+ best activator, 200 mM activates by 100%, increases the affinity of enzyme for NAD+ at high pH Saccharomyces cerevisiae
1.1.1.286 additional information 200 mM Cs+, Li+, and Na+ do not activate Saccharomyces cerevisiae
1.1.1.286 NH4+ 200 mM activates by 80.9% Saccharomyces cerevisiae
1.1.1.286 Rb+ 200 mM activates by 29.3% Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.87 (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ Saccharomyces cerevisiae
-
 2-oxoadipate + NADH + H+ + CO2
-
 ?
1.1.1.286 homoisocitrate + NAD+ Saccharomyces cerevisiae
-
 ? + NADH
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.87 Saccharomyces cerevisiae
-
-
-
1.1.1.286 Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.87 (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
-
 Saccharomyces cerevisiae 2-oxoadipate + NADH + H+ + CO2
-
 ?
1.1.1.87 (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
-
 ?
1.1.1.87 isocitrate + NAD+ low activity Saccharomyces cerevisiae ? + NADH + H+
-
 ?
1.1.1.286 homoisocitrate + NAD+
-
 Saccharomyces cerevisiae ? + NADH
-
 ?
1.1.1.286 isocitrate + NAD+ slow substrate Saccharomyces cerevisiae 2-oxoglutarate + CO2 + NADH + H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.1.87 HIc
-
 Saccharomyces cerevisiae
1.1.1.87 HIc dehydrogenase
-
 Saccharomyces cerevisiae
1.1.1.87 HICDH
-
 Saccharomyces cerevisiae
1.1.1.286 HICDH
-
 Saccharomyces cerevisiae
1.1.1.286 homoisocitrate dehydrogenase
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.87 25
-
 assay at Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.87 8
-
 assay at Saccharomyces cerevisiae

pH Range

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

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.87 NAD+
-
 Saccharomyces cerevisiae
1.1.1.286 NAD+
-
 Saccharomyces cerevisiae

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.1.1.87 77
-
 NAD+ pH 8.0, 25°C, in absence of KOAc Saccharomyces cerevisiae
1.1.1.286 2.7
-
 NADH
-
 Saccharomyces cerevisiae
1.1.1.286 90
-
 Cl-
-
 Saccharomyces cerevisiae
1.1.1.286 500
-
 potassium acetate
-
 Saccharomyces cerevisiae