IDH2
IDH2 (isocitrate dehydrogenase (NADP(+)) 2, also known as IDH-2) is the mitochondrial NADP(+)-dependent isocitrate dehydrogenase. It catalyses the oxidative decarboxylation of isocitrate to 2-oxoglutarate and contributes to intermediary metabolism and energy production. Browse Assay Genie's current range of IDH2 research reagents below, or read on for the biology behind the target.
IDH2 is an isocitrate dehydrogenase, an enzyme that catalyses the oxidative decarboxylation of isocitrate to 2-oxoglutarate. Isocitrate dehydrogenases fall into two subclasses, one using NAD(+) as the electron acceptor and the other using NADP(+). IDH2 belongs to the NADP(+)-dependent subclass and is the form found in mitochondria. It plays a role in intermediary metabolism and energy production, and it may tightly associate or interact with the pyruvate dehydrogenase complex.
Five isocitrate dehydrogenases have been reported in humans: three NAD(+)-dependent enzymes localised to the mitochondrial matrix, and two NADP(+)-dependent enzymes. Of the NADP(+)-dependent pair, IDH2 is mitochondrial, while the other, IDH1, is predominantly cytosolic. Each NADP(+)-dependent isozyme is a homodimer. The IDH2 protein belongs to the isocitrate and isopropylmalate dehydrogenases family, and alternative splicing of the IDH2 gene results in multiple transcript variants.
The HGNC-approved name is isocitrate dehydrogenase (NADP(+)) 2, and the gene sits in the HGNC group of isocitrate dehydrogenases. Earlier names include isocitrate dehydrogenase 2 (NADP+), mitochondrial. Mouse and rat each carry an orthologous Idh2 gene, so the enzyme can be studied across common model organisms. Researchers working on mitochondrial metabolism often study IDH2 alongside IDH1 to compare the two NADP(+)-dependent isozymes.
IDH2 converts isocitrate to 2-oxoglutarate within mitochondria, making it a relevant enzyme for studies of intermediary metabolism.
The enzyme contributes to energy production, so it is a target of interest when examining how mitochondria support cellular energy supply.
IDH2 may tightly associate or interact with the pyruvate dehydrogenase complex, an association that invites further investigation.
Comparing mitochondrial IDH2 with cytosolic IDH1 and the NAD(+)-dependent enzymes helps clarify how the isozymes differ in cofactor use and location.
IDH2 is the mitochondrial NADP(+)-dependent isocitrate dehydrogenase. It catalyses the oxidative decarboxylation of isocitrate to 2-oxoglutarate and plays a role in intermediary metabolism and energy production. It may also tightly associate or interact with the pyruvate dehydrogenase complex.
Both are homodimeric NADP(+)-dependent isocitrate dehydrogenases. IDH2 is found in mitochondria, whereas IDH1 is predominantly cytosolic. Both differ from the three NAD(+)-dependent isocitrate dehydrogenases, which localise to the mitochondrial matrix. Check the datasheet of any product for its validated reactivity.
Yes. Mouse and rat both have an orthologous gene named Idh2. The human enzyme is also known as IDH-2, and the gene produces multiple transcript variants through alternative splicing. Check the datasheet of any product for its validated reactivity.
Other isocitrate dehydrogenase family members and related metabolic enzymes with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P48735; product specifications from Assay Genie datasheets.