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- ***********************************************************
- * Isocitrate and isopropylmalate dehydrogenases signature *
- ***********************************************************
-
- Isocitrate dehydrogenase (IDH) [1,2] 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) [3] catalyzes the third
- step in the biosynthesis of leucine in bacteria and fungi, the oxidative
- decarboxylation of 3-isopropylmalate into 2-oxo-4-methylvalerate.
-
- IDH and IMDH are evolutionary related [1,3]. 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.
-
- -Consensus pattern: N-[LIMVFY]-x-G-D-[LIMVFY]-x-[SG]-[DN]-x(2)-[SA]-x(3,4)-G-
- [SG]-[LIVM]-G-[LIVMF]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
- -Last update: October 1993 / Pattern and text revised.
-
- [ 1] Hurley J.H., Thorsness P.E., Ramalingam V., Helmers N.H.,
- Koshland D.E. Jr., Stroud R.M.
- Proc. Natl. Acad. Sci. U.S.A. 86:8635-8639(1989).
- [ 2] Cupp J.R., McAlister-Henn L.
- J. Biol. Chem. 266:22199-22205(1991).
- [ 3] Imada K., Sato M., Tanaka N., Katsube Y., Matsuura Y., Oshima T.
- J. Mol. Biol. 222:725-738(1991).
-