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Literature summary extracted from

  • Lin, A.P.; McAlister-Henn, L.
    Homologous binding sites in yeast isocitrate dehydrogenase for cofactor (NAD+) and allosteric activator (AMP) (2003), J. Biol. Chem., 278, 12864-12872.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.1.1.41 AMP allosteric activator, binding site at subunit IDH1 Saccharomyces cerevisiae

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.41 expression of His-tagged wild-type and mutant enzymes in yeast strain IDH12DELTAL deficient in both subunits of the enzyme Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.41 D279A/D280A site-directed mutagenesis, mutation of a IDH1 residue, reduced AMP binding, ligand-binding analysis Saccharomyces cerevisiae
1.1.1.41 D286A/I287A site-directed mutagenesis, mutation of a IDH2 residue, highly reduced NAD+ binding, ligand-binding analysis Saccharomyces cerevisiae
1.1.1.41 H281A site-directed mutagenesis, mutation of a IDH2 residue, mutant cannot bind NAD+, ligand-binding analysis Saccharomyces cerevisiae
1.1.1.41 R274A site-directed mutagenesis, mutation of a IDH1 residue, reduced AMP binding, ligand-binding analysis Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.41 additional information
-
 additional information kinetics and ligand binding Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.1.41 mitochondrion
-
 Saccharomyces cerevisiae 5739
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.41 Mg2+ binding site at subunit IDH2, active site Saccharomyces cerevisiae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.41 303000
-
 sequence calculation 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 enzyme performs the rate-limiting step in the mitochondrial tricarboxylic cycle and is subject to complex allosteric regulation 2-oxoglutarate + CO2 + NADH + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.41 Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.41 recombinant His-tagged wild-type and mutant enzymes from strain IDH12DELTAL by nickel affinity chromatography Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.41 D-isocitrate + NAD+ catalytic residues binding isocitrate are located on subunit IDH2, while regulatory residues binding isocitrate are located on subunit IDH1 Saccharomyces cerevisiae 2-oxoglutarate + CO2 + NADH
-
 ?
1.1.1.41 isocitrate + NAD+ enzyme performs the rate-limiting step in the mitochondrial tricarboxylic cycle and is subject to complex allosteric regulation Saccharomyces cerevisiae 2-oxoglutarate + CO2 + NADH + H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.41 octamer alpha4beta4, subunits are termed IDH1 and IDH2 Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
1.1.1.41 IDH
-
 Saccharomyces cerevisiae
1.1.1.41 isocitrate dehydrogenase
-
 Saccharomyces cerevisiae
1.1.1.41 NAD+-specific isocitrate dehydrogenase
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.41 24
-
 assay at Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.41 7.4
-
 assay at Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.41 NAD+ specific for, binding site at subunit IDH2 Saccharomyces cerevisiae