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Literature summary for 1.1.1.41 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

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ activates Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
isocitrate + NAD+ Homo sapiens
-
2-oxoglutarate + CO2 + NADH + H+
-
?

Organism

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
NAD-dependent isocitrate dehydrogenase
-
Homo sapiens
NAD-IDH
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Homo sapiens