| Family: | DECARBOXYLATING DEHYDROGENASES-ISOCITRATE, ISOPROPYLMALATE, TARTRATE (PTHR11835) | ||
| Subfamilies: | 11 | ||
| PANTHER Links: |
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| Abstract: |
Isocitrate dehydrogenase (IDH) [PMID:2682654, PMID:1939242] is an important enzyme of carbohydrate metabolism which catalyzes the oxidative decarboxylation of isocitrate into alpha-ketoglutarate. IDH is either dependent on NAD+ (EC: 1.1.1.41) or on NADP+ (EC: 1.1.1.42). 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: 1.1.1.85) (IMDH) [PMID:1748999, PMID:7773180] catalyzes 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: 1.1.1.93) [PMID:8053675] catalyzes the reduction of tartrate to oxaloglycolate. These enzymes are evolutionary related [PMID:2682654, PMID:1748999, PMID:7773180, PMID:8053675]. The best conserved region of these enzymes is a glycine-rich stretch of residues located in the C-terminal section. |
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| InterPro Accession: | IPR001804 | ||
| PANTHER Molecular Function: |
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| PANTHER Biological Process: |
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| Pathway Categories: | No pathway information available | ||
| Training Sequences: |
178
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| HMM Length | 353 | ||
| Downloads: | HMM (HMMER format) |
| Total | Celera | FlyBase | NCBI | |
| H. sapiens | 7 | 4 | 0 | 3 |
| M. musculus | 8 | 4 | 0 | 4 |
| R. norvegicus | 7 | 4 | 0 | 3 |
| D. melanogaster | 6 | 0 | 6 | 0 |




