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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.
    View publication on PubMedView publication on EuropePMC

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