| Description | Isocitrate dehydrogenase (IDH) [ , ] is an important enzyme of carbohydrate metabolism which catalyses the oxidative decarboxylation of isocitrate into alpha-ketoglutarate. IDH is either dependent on NAD+( ) or on NADP +( ). 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 ( ) (IMDH) [ , ] 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 ( ) [ ] catalyses the reduction of tartrate to oxaloglycolate.These enzymes are evolutionary related [ , , , ]. 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. | Name | Isocitrate/isopropylmalate dehydrogenase, conserved site |
| Short Name | IsoCit/isopropylmalate_DH_CS | Type | Conserved_site |
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