D
IPR024084

Isopropylmalate dehydrogenase-like domain

InterPro entry
Short nameIsoPropMal-DH-like_dom

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
[4, 2]
. IDH is either dependent on NAD+ (
1.1.1.41
) or on NADP+ (
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.

IMDH (
1.1.1.85
) catalyses the third step in the biosynthesis of leucine in bacteria and fungi, the oxidative decarboxylation of 3-isopropylmalate into 2-oxo-4-methylvalerate
[5, 3]
.

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
[1]
.

References

1.Crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus. Wallon G, Kryger G, Lovett ST, Oshima T, Ringe D, Petsko GA. J. Mol. Biol. 266, 1016-31, (1997). View articlePMID: 9086278

2.NAD(+)-dependent isocitrate dehydrogenase. Cloning, nucleotide sequence, and disruption of the IDH2 gene from Saccharomyces cerevisiae. Cupp JR, McAlister-Henn L. J. Biol. Chem. 266, 22199-205, (1991). View articlePMID: 1939242

3.Modeling substrate binding in Thermus thermophilus isopropylmalate dehydrogenase. Zhang T, Koshland DE Jr. Protein Sci. 4, 84-92, (1995). View articlePMID: 7773180

4.Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase. Hurley JH, Thorsness PE, Ramalingam V, Helmers NH, Koshland DE Jr, Stroud RM. Proc. Natl. Acad. Sci. U.S.A. 86, 8635-9, (1989). View articlePMID: 2682654

5.Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 A resolution. Imada K, Sato M, Tanaka N, Katsube Y, Matsuura Y, Oshima T. J. Mol. Biol. 222, 725-38, (1991). View articlePMID: 1748999

Further reading

6. Tartrate dehydrogenase, a new member of the family of metal-dependent decarboxylating R-hydroxyacid dehydrogenases. Tipton PA, Beecher BS. Arch. Biochem. Biophys. 313, 15-21, (1994). View articlePMID: 8053675

Cross References

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