Literature summary extracted from
McAlister-Henn, L.
Ligand binding and structural changes associated with allostery in yeast NAD+-specific isocitrate dehydrogenase (2012), Arch. Biochem. Biophys., 519, 112-117.
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
1.1.1.41 |
AMP |
allosteric activation, binds to subunit IDH1 |
Saccharomyces cerevisiae |
|
Protein Variants
EC Number |
Protein Variants |
Comment |
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 |
Comment |
Organism |
Structure |
---|
1.1.1.41 |
Mg2+ |
required |
Saccharomyces cerevisiae |
|
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
1.1.1.41 |
isocitrate + NAD+ |
Saccharomyces cerevisiae |
- |
2-oxoglutarate + CO2 + NADH + H+ |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.1.1.41 |
Saccharomyces cerevisiae |
- |
- |
- |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
1.1.1.41 |
isocitrate + NAD+ |
- |
Saccharomyces cerevisiae |
2-oxoglutarate + CO2 + NADH + H+ |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
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 |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.1.1.41 |
NAD+-specific isocitrate dehydrogenase |
- |
Saccharomyces cerevisiae |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
1.1.1.41 |
NAD+ |
- |
Saccharomyces cerevisiae |
|
General Information
EC Number |
General Information |
Comment |
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 |