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Isocitrate dehydrogenase (IDH) [1,2] is an important enzyme of carbohydrate metabolism which catalyzes the oxidative decarboxylation of isocitrate into α-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) [3,4] 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) [5] catalyzes the reduction of tartrate to oxaloglycolate.

These enzymes are evolutionary related [1,3,4,5]. The best conserved region of these enzymes is a glycine-rich stretch of residues located in the C-terminal section. We have used this region as a signature pattern.

December 2004 / Pattern and text revised.

PROSITE method (with tools and information) covered by this documentation:

IDH_IMDH, PS00470; Isocitrate and isopropylmalate dehydrogenases signature  (PATTERN)

Consensus pattern: [NSK]-[LIMYTV]-[FYDNH]-[GEA]-[DNGSTY]-[IMVYL]-x-[STGDN]-[DN]-x(1,2)-[SGAP]-x(3,4)-[GE]-[STG]-[LIVMPA]-[GA]-[LIVMF] Sequences known to belong to this class detected by the pattern: ALL Other sequence(s) detected in Swiss-Prot: NONE

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00470 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00470 • Scan Swiss-Prot/TrEMBL entries against PS00470 • view ligand binding statistics

Matching PDB structures: 1A05 1AI2 1AI3 1BL5 ... [ALL]

1	Authors	Hurley J.H., Thorsness P.E., Ramalingam V., Helmers N.H., Koshland D.E. Jr., Stroud R.M.
	Title	Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase.
	Source	Proc. Natl. Acad. Sci. U.S.A. 86:8635-8639(1989).
	PubMed ID	2682654

2	Authors	Cupp J.R., McAlister-Henn L.
	Title	NAD(+)-dependent isocitrate dehydrogenase. Cloning, nucleotide sequence, and disruption of the IDH2 gene from Saccharomyces cerevisiae.
	Source	J. Biol. Chem. 266:22199-22205(1991).
	PubMed ID	1939242

3	Authors	Imada K., Sato M., Tanaka N., Katsube Y., Matsuura Y., Oshima T.
	Title	Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 A resolution.
	Source	J. Mol. Biol. 222:725-738(1991).
	PubMed ID	1748999

4	Authors	Zhang T., Koshland D.E. Jr.
	Title	Modeling substrate binding in Thermus thermophilus isopropylmalate dehydrogenase.
	Source	Protein Sci. 4:84-92(1995).
	PubMed ID	7773180

5	Authors	Tipton P.A., Beecher B.S.
	Title	Tartrate dehydrogenase, a new member of the family of metal-dependent decarboxylating R-hydroxyacid dehydrogenases.
	Source	Arch. Biochem. Biophys. 313:15-21(1994).
	PubMed ID	8053675

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