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Literature summary extracted from

  • Gross, S.; Cairns, R.A.; Minden, M.D.; Driggers, E.M.; Bittinger, M.A.; Jang, H.G.; Sasaki, M.; Jin, S.; Schenkein, D.P.; Su, S.M.; Dang, L.; Fantin, V.R.; Mak, T.W.
    Cancer-associated metabolite 2-hydroxyglutarate accumulates in acute myelogenous leukemia with isocitrate dehydrogenase 1 and 2 mutations (2010), J. Exp. Med., 207, 339-344.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.42 IDH1, genotyping in acute myelogenous leukemia patients, overview Homo sapiens
1.1.1.42 IDH2, genotyping in acute myelogenous leukemia patients, overview Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.42 R132C IDH1 R132 mutations cause production and accumulation of 2-hydroxyglutarate in acute myelogenous leukemia cells. The mutation reduces the affinity for isocitrate, and increases the affinity for NADPH and 2-oxoglutarate, preventing the oxidative decarboxylation of isocitrate to 2-oxoglutarate, and facilitating the conversion of 2-oxoglutarate to 2-hydroxyglutarate Homo sapiens
1.1.1.42 R132G IDH1 R132 mutations cause production and accumulation of 2-hydroxyglutarate in acute myelogenous leukemia cells Homo sapiens
1.1.1.42 R132H IDH1 R132 mutations cause production and accumulation of 2-hydroxyglutarate in acute myelogenous leukemia cells Homo sapiens
1.1.1.42 R172K IDH2 R172 mutation causes production and accumulation of 2-hydroxyglutarate in acute myelogenous leukemia cells Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.1.42 cytosol IDH1 Homo sapiens 5829
-
1.1.1.42 mitochondrion IDH2 Homo sapiens 5739
-
1.1.1.42 peroxisome IDH1 Homo sapiens 5777
-

Metals/Ions

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.42 isocitrate + NADP+ Homo sapiens
-
2-oxoglutarate + NADPH + H+ + CO2
-
r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.42 Homo sapiens O75874 IDH1
-
1.1.1.42 Homo sapiens P48735 IDH2
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.1.42 glioblastoma cell multiforme tumors Homo sapiens
-
1.1.1.42 glioma cell
-
Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.42 isocitrate + NADP+
-
Homo sapiens 2-oxoglutarate + NADPH + H+ + CO2
-
r

Synonyms

EC Number Synonyms Comment Organism
1.1.1.42 IDH1
-
Homo sapiens
1.1.1.42 IDH2
-
Homo sapiens
1.1.1.42 isocitrate dehydrogenase 1
-
Homo sapiens
1.1.1.42 isocitrate dehydrogenase 2
-
Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.42 7.5
-
assay at Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.42 NADP+
-
Homo sapiens
1.1.1.42 NADPH
-
Homo sapiens

General Information

EC Number General Information Comment Organism
1.1.1.42 metabolism IDH1 is critical in cellular metabolism Homo sapiens
1.1.1.42 physiological function mutation at R172 in the active site of IDH2 leads to a change in the molecular mechanism of enzyme catalysis, resulting in production and accumulation of elevated 2-hydroxyglutarate in acute myelogenous leukemia. The mutation reduces the affinity for isocitrate, and increases the affinity for NADPH and 2-oxoglutarate, preventing the oxidative decarboxylation of isocitrate to 2-oxoglutarate, and facilitating the conversion of 2-oxoglutarate to 2-hydroxyglutarate Homo sapiens
1.1.1.42 physiological function mutations at R132 in the active site of IDH1 lead to a change in the molecular mechanism of enzyme catalysis, resulting in production and accumulation of elevated 2-hydroxyglutarate in acute myelogenous leukemia. The mutations reduce the affinity for isocitrate, and increase the affinity for NADPH and 2-oxoglutarate, preventing the oxidative decarboxylation of isocitrate to 2-oxoglutarate, and facilitating the conversion of 2-oxoglutarate to 2-hydroxyglutarate Homo sapiens