BRENDA - Enzyme Database

Ligand binding and structural changes associated with allostery in yeast NAD+-specific isocitrate dehydrogenase

McAlister-Henn, L.; Arch. Biochem. Biophys. 519, 112-117 (2012)

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
Organism
Structure
1.1.1.41
AMP
allosteric activation, binds to subunit IDH1
Saccharomyces cerevisiae
Engineering
EC Number
Amino acid exchange
Commentary
Organism
1.1.1.41
C150S
site-directed mutagenesis of subunit IDH2, disulfide bridge formation by C150 is abolished
Saccharomyces cerevisiae
1.1.1.41
C56S/C242S
site-directed mutagenesis of subunit IDH2, the mutation does not affect disulfide formation in the enzyme
Saccharomyces cerevisiae
1.1.1.41
D279A
site-directed mutagenesis of subunit IDH1, the mutation results in a loss of activation by AMP
Saccharomyces cerevisiae
1.1.1.41
D286A
site-directed mutagenesis of subunit IDH2, the mutation results in a dramatic reduction in Vmax primarily due to a 70fold increase in the S0.5 value for NAD+
Saccharomyces cerevisiae
1.1.1.41
G15D
site-directed mutagenesis of subunit IDH1, the tetrameric IDH1G15D/IDH2 enzyme exhibits half-site binding (two sites) for isocitrate in the absence of DTT and full-site binding (four sites) in the presence of DTT
Saccharomyces cerevisiae
1.1.1.41
I280A
site-directed mutagenesis of subunit IDH1, the mutation results in a loss of activation by AMP
Saccharomyces cerevisiae
1.1.1.41
I287A
site-directed mutagenesis of subunit IDH2, the mutation results in a dramatic reduction in Vmax primarily due to a 70fold increase in the S0.5 value for NAD+
Saccharomyces cerevisiae
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
1.1.1.41
Mg2+
required
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.1.1.41
isocitrate + NAD+
Saccharomyces cerevisiae
-
2-oxoglutarate + CO2 + NADH
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.1.1.41
Saccharomyces cerevisiae
-
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.1.1.41
isocitrate + NAD+
-
721433
Saccharomyces cerevisiae
2-oxoglutarate + CO2 + NADH
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
1.1.1.41
More
subunit IDH2 contains catalytic isocitrate/Mg2+ and NAD+ binding sites whereas subunit IDH1 contains homologous binding sites, respectively, for cooperative binding of isocitrate and for allosteric binding of AMP. The subsunits share 42% sequence identity
Saccharomyces cerevisiae
1.1.1.41
octamer
4 * regulatory IDH1 + 4 * catalytic IDH2 subunits
Saccharomyces cerevisiae
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.1.1.41
NAD+
-
Saccharomyces cerevisiae
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
Organism
Structure
1.1.1.41
AMP
allosteric activation, binds to subunit IDH1
Saccharomyces cerevisiae
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.1.1.41
NAD+
-
Saccharomyces cerevisiae
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
1.1.1.41
C150S
site-directed mutagenesis of subunit IDH2, disulfide bridge formation by C150 is abolished
Saccharomyces cerevisiae
1.1.1.41
C56S/C242S
site-directed mutagenesis of subunit IDH2, the mutation does not affect disulfide formation in the enzyme
Saccharomyces cerevisiae
1.1.1.41
D279A
site-directed mutagenesis of subunit IDH1, the mutation results in a loss of activation by AMP
Saccharomyces cerevisiae
1.1.1.41
D286A
site-directed mutagenesis of subunit IDH2, the mutation results in a dramatic reduction in Vmax primarily due to a 70fold increase in the S0.5 value for NAD+
Saccharomyces cerevisiae
1.1.1.41
G15D
site-directed mutagenesis of subunit IDH1, the tetrameric IDH1G15D/IDH2 enzyme exhibits half-site binding (two sites) for isocitrate in the absence of DTT and full-site binding (four sites) in the presence of DTT
Saccharomyces cerevisiae
1.1.1.41
I280A
site-directed mutagenesis of subunit IDH1, the mutation results in a loss of activation by AMP
Saccharomyces cerevisiae
1.1.1.41
I287A
site-directed mutagenesis of subunit IDH2, the mutation results in a dramatic reduction in Vmax primarily due to a 70fold increase in the S0.5 value for NAD+
Saccharomyces cerevisiae
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
1.1.1.41
Mg2+
required
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
1.1.1.41
isocitrate + NAD+
Saccharomyces cerevisiae
-
2-oxoglutarate + CO2 + NADH
-
-
?
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.1.1.41
isocitrate + NAD+
-
721433
Saccharomyces cerevisiae
2-oxoglutarate + CO2 + NADH
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.1.1.41
More
subunit IDH2 contains catalytic isocitrate/Mg2+ and NAD+ binding sites whereas subunit IDH1 contains homologous binding sites, respectively, for cooperative binding of isocitrate and for allosteric binding of AMP. The subsunits share 42% sequence identity
Saccharomyces cerevisiae
1.1.1.41
octamer
4 * regulatory IDH1 + 4 * catalytic IDH2 subunits
Saccharomyces cerevisiae
General Information
EC Number
General Information
Commentary
Organism
1.1.1.41
metabolism
yeast IDH is regulated both by allostery and by covalent formation of a disulfide bond, and these regulatory mechanisms contribute to modulation of respiratory metabolism in vivo
Saccharomyces cerevisiae
General Information (protein specific)
EC Number
General Information
Commentary
Organism
1.1.1.41
metabolism
yeast IDH is regulated both by allostery and by covalent formation of a disulfide bond, and these regulatory mechanisms contribute to modulation of respiratory metabolism in vivo
Saccharomyces cerevisiae