BRENDA - Enzyme Database

Potassium is an activator of homoisocitrate dehydrogenase from Saccharomyces cerevisiae

Lin, Y.; West, A.H.; Cook, P.F.; Biochemistry 47, 10809-10815 (2008)

Data extracted from this reference:

Inhibitors
EC Number
Inhibitors
Commentary
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
Commentary
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
Commentary
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
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
Primary Accession No. (UniProt)
Commentary
Textmining
1.1.1.87
Saccharomyces cerevisiae
-
-
-
1.1.1.286
Saccharomyces cerevisiae
-
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.1.1.87
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
-
696220
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+
696220
Saccharomyces cerevisiae
2-oxoadipate + NADH + H+ + CO2
-
-
-
?
1.1.1.87
isocitrate + NAD+
low activity
696220
Saccharomyces cerevisiae
? + NADH + H+
-
-
-
?
1.1.1.286
homoisocitrate + NAD+
-
696220
Saccharomyces cerevisiae
? + NADH
-
-
-
?
1.1.1.286
isocitrate + NAD+
slow substrate
696220
Saccharomyces cerevisiae
2-oxoglutarate + CO2 + NADH
-
-
-
?
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
1.1.1.87
25
-
assay at
Saccharomyces cerevisiae
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.1.1.87
8
-
assay at
Saccharomyces cerevisiae
pH Range
EC Number
pH Minimum
pH Maximum
Commentary
Organism
1.1.1.87
additional information
-
pH-rate profile in the absence of K+, overview
Saccharomyces cerevisiae
Cofactor
EC Number
Cofactor
Commentary
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
Commentary
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
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.1.1.87
NAD+
-
Saccharomyces cerevisiae
1.1.1.286
NAD+
-
Saccharomyces cerevisiae
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
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
Ki Value [mM] (protein specific)
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
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
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
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 (protein specific)
EC Number
Metals/Ions
Commentary
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) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
-
-
?
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.1.1.87
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
-
696220
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+
696220
Saccharomyces cerevisiae
2-oxoadipate + NADH + H+ + CO2
-
-
-
?
1.1.1.87
isocitrate + NAD+
low activity
696220
Saccharomyces cerevisiae
? + NADH + H+
-
-
-
?
1.1.1.286
homoisocitrate + NAD+
-
696220
Saccharomyces cerevisiae
? + NADH
-
-
-
?
1.1.1.286
isocitrate + NAD+
slow substrate
696220
Saccharomyces cerevisiae
2-oxoglutarate + CO2 + NADH
-
-
-
?
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
1.1.1.87
25
-
assay at
Saccharomyces cerevisiae
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.1.1.87
8
-
assay at
Saccharomyces cerevisiae
pH Range (protein specific)
EC Number
pH Minimum
pH Maximum
Commentary
Organism
1.1.1.87
additional information
-
pH-rate profile in the absence of K+, overview
Saccharomyces cerevisiae