Activating Compound | Comment | Organism | Structure |
---|---|---|---|
AMP | allosteric activation, binds to subunit IDH1 | Saccharomyces cerevisiae |
Protein Variants | Comment | Organism |
---|---|---|
C150S | site-directed mutagenesis of subunit IDH2, disulfide bridge formation by C150 is abolished | Saccharomyces cerevisiae |
C56S/C242S | site-directed mutagenesis of subunit IDH2, the mutation does not affect disulfide formation in the enzyme | Saccharomyces cerevisiae |
D279A | site-directed mutagenesis of subunit IDH1, the mutation results in a loss of activation by AMP | Saccharomyces cerevisiae |
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 |
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 |
I280A | site-directed mutagenesis of subunit IDH1, the mutation results in a loss of activation by AMP | Saccharomyces cerevisiae |
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 | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
isocitrate + NAD+ | Saccharomyces cerevisiae | - |
2-oxoglutarate + CO2 + NADH + H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
isocitrate + NAD+ | - |
Saccharomyces cerevisiae | 2-oxoglutarate + CO2 + NADH + H+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
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 |
octamer | 4 * regulatory IDH1 + 4 * catalytic IDH2 subunits | Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
NAD+-specific isocitrate dehydrogenase | - |
Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Saccharomyces cerevisiae |
General Information | Comment | Organism |
---|---|---|
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 |