Isocitrate dehydrogenase NADP-dependent (IPR004790)

Short name: Isocitrate_DH_NADP

Overlapping homologous superfamilies


Family relationships



Isocitrate dehydrogenase (IDH) [PMID: 2682654, PMID: 1939242] is an important enzyme of carbohydrate metabolism which catalyzes the oxidative decarboxylation of isocitrate into alpha-ketoglutarate. IDH is either dependent on NAD+ (EC: or on NADP+ (EC: In eukaryotes there are at least three isozymes of IDH: two are located in the mitochondrial matrix (one NAD+-dependent, the other NADP+-dependent), while the third one (also NADP+-dependent) is cytoplasmic. In Escherichia coli the activity of a NADP+-dependent form of the enzyme is controlled by the phosphorylation of a serine residue; the phosphorylated form of IDH is completely inactivated.

The eukaryotic, NADP-dependent isocitrate dehydrogenases, are defined by this family that includes cytosolic, mitochondrial, and chloroplast enzymes, as well as bacterial proteins. This family differs considerably from other isocitrate dehydrogenases that are included in a different group together with 3-isopropylmalate dehydrogenases and tartrate dehydrogenases.

GO terms

Biological Process

GO:0006102 isocitrate metabolic process
GO:0055114 oxidation-reduction process

Molecular Function

GO:0004450 isocitrate dehydrogenase (NADP+) activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.