BRENDA - Enzyme Database
show all sequences of 1.1.1.286

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
Inhibitors
Commentary
Organism
Structure
3-carboxypropylidenemalate
-
Saccharomyces cerevisiae
Cl-
-
Saccharomyces cerevisiae
NADH
product inhibitor
Saccharomyces cerevisiae
potassium acetate
-
Saccharomyces cerevisiae
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
K+
best activator, 200 mM activates by 100%, increases the affinity of enzyme for NAD+ at high pH
Saccharomyces cerevisiae
additional information
200 mM Cs+, Li+, and Na+ do not activate
Saccharomyces cerevisiae
NH4+
200 mM activates by 80.9%
Saccharomyces cerevisiae
Rb+
200 mM activates by 29.3%
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
homoisocitrate + NAD+
Saccharomyces cerevisiae
-
? + NADH
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Saccharomyces cerevisiae
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
homoisocitrate + NAD+
-
696220
Saccharomyces cerevisiae
? + NADH
-
-
-
?
isocitrate + NAD+
slow substrate
696220
Saccharomyces cerevisiae
2-oxoglutarate + CO2 + NADH
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Saccharomyces cerevisiae
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
2.7
-
NADH
-
Saccharomyces cerevisiae
90
-
Cl-
-
Saccharomyces cerevisiae
500
-
potassium acetate
-
Saccharomyces cerevisiae
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Saccharomyces cerevisiae
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
3-carboxypropylidenemalate
-
Saccharomyces cerevisiae
Cl-
-
Saccharomyces cerevisiae
NADH
product inhibitor
Saccharomyces cerevisiae
potassium acetate
-
Saccharomyces cerevisiae
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
2.7
-
NADH
-
Saccharomyces cerevisiae
90
-
Cl-
-
Saccharomyces cerevisiae
500
-
potassium acetate
-
Saccharomyces cerevisiae
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
K+
best activator, 200 mM activates by 100%, increases the affinity of enzyme for NAD+ at high pH
Saccharomyces cerevisiae
additional information
200 mM Cs+, Li+, and Na+ do not activate
Saccharomyces cerevisiae
NH4+
200 mM activates by 80.9%
Saccharomyces cerevisiae
Rb+
200 mM activates by 29.3%
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
homoisocitrate + NAD+
Saccharomyces cerevisiae
-
? + NADH
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
homoisocitrate + NAD+
-
696220
Saccharomyces cerevisiae
? + NADH
-
-
-
?
isocitrate + NAD+
slow substrate
696220
Saccharomyces cerevisiae
2-oxoglutarate + CO2 + NADH
-
-
-
?
Other publictions for EC 1.1.1.286
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
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1
1
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1
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4
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1
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1
1
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16
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6
1
1
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2
1
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2
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1
2
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2
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6
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1
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6
1
1
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2
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8
1
1
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2
1
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2
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1
2
1
-
-
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1
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2
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1
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6
-
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1
-
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8
1
1
-
-
2
1
-
-
-
-
3
3
-
2
2
685232
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Chemical mechanism of homoisoc ...
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Biochemistry
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4169-4180
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-
-
-
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3
1
-
-
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1
-
1
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2
-
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3
-
1
-
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-
1
1
-
1
1
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-
1
-
-
-
-
3
1
1
-
-
-
1
-
-
-
-
-
-
-
-
3
-
1
-
-
-
1
1
-
-
-
-
-
-
-
-
696220
Lin
Potassium is an activator of h ...
Saccharomyces cerevisiae
Biochemistry
47
10809-10815
2008
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4
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4
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1
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1
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2
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1
3
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1
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4
3
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4
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1
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2
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1
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3
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3
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1
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1
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4
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3
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5
1
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8
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1
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1
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4
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3
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8
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3
3
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5
1
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8
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656127
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Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
J. Biol. Chem.
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2003
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1
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1
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2
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2
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6
1
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1
2
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1
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1
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6
1
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2
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