v5.1.0.3
Glycine data from LIS
Type | Family |
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. 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. |
Short Name | Isocitrate_DH_NADP |