Conserved Site

Isocitrate/isopropylmalate dehydrogenase, conserved site (IPR019818)

Short name: IsoCit/isopropylmalate_DH_CS


Isocitrate dehydrogenase (IDH) [PMID: 2682654, PMID: 1939242] is an important enzyme of carbohydrate metabolism which catalyses 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.

3-isopropylmalate dehydrogenase (EC: (IMDH) [PMID: 1748999, PMID: 7773180] catalyses the third step in the biosynthesis of leucine in bacteria and fungi, the oxidative decarboxylation of 3-isopropylmalate into 2-oxo-4-methylvalerate. Tartrate dehydrogenase (EC: [PMID: 8053675] catalyses the reduction of tartrate to oxaloglycolate.

These enzymes are evolutionary related [PMID: 2682654, PMID: 1748999, PMID: 7773180, PMID: 8053675]. The signature pattern of this entry is located in a conserved region, which contains a glycine-rich stretch of residues located in the C-terminal section.

GO terms

Biological Process

GO:0055114 oxidation-reduction process

Molecular Function

GO:0051287 NAD binding
GO:0000287 magnesium ion binding
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor

Cellular Component

No terms assigned in this category.

Contributing signatures

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