Summary: Isocitrate/isopropylmalate dehydrogenase
This is the Wikipedia entry entitled "Isocitrate/isopropylmalate dehydrogenase family". More...
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Isocitrate/isopropylmalate dehydrogenase family Edit Wikipedia article
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crystal structure of k230m isocitrate dehydrogenase in complex with alpha-ketoglutarate
In molecular biology, the isocitrate/isopropylmalate dehydrogenase family is a protein family consisting of the evolutionary related enzymes isocitrate dehydrogenase, 3-isopropylmalate dehydrogenase and tartrate dehydrogenase.
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+ EC 188.8.131.52 or on NADP+ EC 184.108.40.206. 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 220.127.116.11 (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.
- Hurley JH, Thorsness PE, Ramalingam V, Helmers NH, Koshland DE, Stroud RM (November 1989). "Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase". Proc. Natl. Acad. Sci. U.S.A. 86 (22): 8635–9. doi:10.1073/pnas.86.22.8635. PMC 298342. PMID 2682654.
- Imada K, Sato M, Tanaka N, Katsube Y, Matsuura Y, Oshima T (December 1991). "Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 A resolution". J. Mol. Biol. 222 (3): 725–38. doi:10.1016/0022-2836(91)90508-4. PMID 1748999.
- Zhang T, Koshland DE (January 1995). "Modeling substrate binding in Thermus thermophilus isopropylmalate dehydrogenase". Protein Sci. 4 (1): 84–92. doi:10.1002/pro.5560040111. PMC 2142962. PMID 7773180.
- Tipton PA, Beecher BS (August 1994). "Tartrate dehydrogenase, a new member of the family of metal-dependent decarboxylating R-hydroxyacid dehydrogenases". Arch. Biochem. Biophys. 313 (1): 15–21. doi:10.1006/abbi.1994.1352. PMID 8053675.
- Cupp JR, McAlister-Henn L (November 1991). "NAD(+)-dependent isocitrate dehydrogenase. Cloning, nucleotide sequence, and disruption of the IDH2 gene from Saccharomyces cerevisiae". J. Biol. Chem. 266 (33): 22199–205. PMID 1939242.
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External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR024084
Isocitrate dehydrogenase (IDH) [PUBMED:2682654, PUBMED:1939242] is an important enzyme of carbohydrate metabolism which catalyses the oxidative decarboxylation of isocitrate into alpha-ketoglutarate. IDH is either dependent on NAD+ (EC) or on NADP+ (EC). 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) (IMDH) [PUBMED:1748999, PUBMED:7773180] 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 (EC) [PUBMED:8053675] catalyses the reduction of tartrate to oxaloglycolate.
These enzymes are evolutionary related. To this family also belongs the enzyme tartrate dehydrogenase, which shows strong homology to prokaryotic isopropylmalate dehydrogenases and, to a lesser extent, isocitrate dehydrogenase [PUBMED:8053675].
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 [PUBMED:9086278].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor (GO:0016616)|
|Biological process||oxidation-reduction process (GO:0055114)|
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|Number in seed:||23|
|Number in full:||12354|
|Average length of the domain:||320.30 aa|
|Average identity of full alignment:||29 %|
|Average coverage of the sequence by the domain:||93.82 %|
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build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||15|
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