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Literature summary for 1.1.1.41 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

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

Cloned(Commentary)

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

Protein Variants

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

KM Value [mM]

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

Localization

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

Metals/Ions

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
303000
-
sequence calculation Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
?
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

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

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

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