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Literature summary extracted from

  • Lin, A.P.; McAlister-Henn, L.
    Isocitrate binding at two functionally distinct sites in yeast NAD+-specific isocitrate dehydrogenase (2002), J. Biol. Chem., 277, 22475-22483.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.1.1.41 AMP allosteric activation 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 A108R/F136Y/T241D/N245D site-directed mutagenesis, residues of subunit IDH1 mutant is unable to bind AMP, ligand-binding analysis Saccharomyces cerevisiae
1.1.1.41 A108R/F136Y/T241D/N245D/R114A/Y142F/D248T/D252N site-directed mutagenesis, residues of subunit IDH1 are A108R, F136Y, T241D, and N245D, residues of subunit IDH2 are R114A, Y142F, D248T, and D252N, mutant is unable to bind AMP, ligand-binding analysis Saccharomyces cerevisiae
1.1.1.41 R114A/Y142F/D248T/D252N site-directed mutagenesis, residues of subunit subunit IDH2, ligand-binding analysis Saccharomyces cerevisiae
1.1.1.41 S92A site-directed mutagenesis, residue of subunit IDH1, reduction of isocitrate substrate binding sites by half, detrimental effects on isocitrate binding and respective kinetic defects in catalysis and allosteric activation by AMP, ligand-binding analysis Saccharomyces cerevisiae
1.1.1.41 S92A/S98A site-directed mutagenesis, residue of subunit IDH1 is S92, residue of subunit IDH2 is S98, ligand-binding analysis Saccharomyces cerevisiae
1.1.1.41 S98A site-directed mutagenesis, residue of subunit IDH2, reduction of isocitrate substrate binding sites by half, detrimental effects on isocitrate binding and respective kinetic defects in catalysis and allosteric activation by AMP, 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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.41 Mg2+
-
 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 DL-isocitrate + NAD+ Saccharomyces cerevisiae
-
 2-oxoglutarate + CO2 + NADH
-
 ?

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

Storage Stability

EC Number Storage Stability Organism
1.1.1.41 4°C, recombinant wild-type enzyme, in affinity elution buffer containing 50 mM sodium phosphate, pH 7.5, 300 mM NaCl, and 200 mM imidazole, stable for several weeks Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.41 DL-isocitrate + NAD+
-
 Saccharomyces cerevisiae 2-oxoglutarate + CO2 + NADH
-
 ?
1.1.1.41 DL-isocitrate + NAD+ isocitrate binds at 2 functionally distinct sites Saccharomyces cerevisiae 2-oxoglutarate + CO2 + NADH
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.41 More model of binding sites for isocitrate of the 2 different subunits Saccharomyces cerevisiae
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 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 Saccharomyces cerevisiae