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Literature summary extracted from

  • Ma, T.; Peng, Y.; Huang, W.; Ding, J.
    Molecular mechanism of the allosteric regulation of the alphagamma heterodimer of human NAD-dependent isocitrate dehydrogenase (2017), Sci. Rep., 7, 40921 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.1.1.41 ADP the alpha2betagamma heterotetramer and alphagamma heterodimer can be allosterically activated by ADP Homo sapiens
1.1.1.41 citrate the alpha2betagamma heterotetramer and alphagamma heterodimer can be allosterically activated by citrate Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.41 Mg2+ activates Homo sapiens

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+ Homo sapiens
-
 2-oxoglutarate + CO2 + NADH + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.41 Homo sapiens P50213 and O43837 and P51553 subunits alpha, beta and gamma
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.41 isocitrate + NAD+
-
 Homo sapiens 2-oxoglutarate + CO2 + NADH + H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.1.41 NAD-dependent isocitrate dehydrogenase
-
 Homo sapiens
1.1.1.41 NAD-IDH
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.41 NAD+
-
 Homo sapiens