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Literature summary for 1.1.1.41 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

Activating Compound Comment Organism Structure
AMP allosteric activation 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
A108R/F136Y/T241D/N245D site-directed mutagenesis, residues of subunit IDH1 mutant is unable to bind AMP, ligand-binding analysis Saccharomyces cerevisiae
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
R114A/Y142F/D248T/D252N site-directed mutagenesis, residues of subunit subunit IDH2, ligand-binding analysis Saccharomyces cerevisiae
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
S92A/S98A site-directed mutagenesis, residue of subunit IDH1 is S92, residue of subunit IDH2 is S98, ligand-binding analysis Saccharomyces cerevisiae
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]

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
DL-isocitrate + NAD+ Saccharomyces cerevisiae
-
2-oxoglutarate + CO2 + NADH
-
?

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

Storage Stability

Storage Stability Organism
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)

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

Subunits

Subunits Comment Organism
More model of binding sites for isocitrate of the 2 different subunits Saccharomyces cerevisiae
octamer alpha4beta4, subunits are termed IDH1 and IDH2 Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
IDH
-
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 Saccharomyces cerevisiae