| Description | The isocitrate and isopropylmalate dehydrogenases family includes isocitrate dehydrogenase (IDH), 3-isopropylmalate dehydrogenase (IMDH) and tartrate 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. 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 [ , ].This entry represents a structural domain found in all types of isocitrate dehydrogenase, and in isopropylmalate dehydrogenase and tartrate dehydrogenase. The crystal structure of Escherichia coli isopropylmalate dehydrogenase has been described [ ]. | Name | Isopropylmalate dehydrogenase-like domain |
| Short Name | IsoPropMal-DH-like_dom | Type | Domain |
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