LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Type | Domain |
| 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 [ , ]. Tartrate dehydrogenase ( ) shows strong homology to prokaryotic isopropylmalate dehydrogenases and, to a lesser extent, isocitrate dehydrogenase [ ]. It catalyses the reduction of tartrate to oxaloglycolate [].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 [ ]. |
| Short Name | IsoPropMal-DH-like_dom |
