IDH1
IDH1 (isocitrate dehydrogenase (NADP(+)) 1) is the cytoplasmic and peroxisomal NADP(+)-dependent isocitrate dehydrogenase. It catalyses the oxidative decarboxylation of isocitrate to 2-oxoglutarate and is a major source of cytoplasmic NADPH. Browse Assay Genie's current range of IDH1 research reagents below, or read on for the biology behind the target.
IDH1 catalyses the NADP(+)-dependent oxidative decarboxylation of isocitrate (D-threo-isocitrate) to 2-ketoglutarate, also called 2-oxoglutarate. This product is required by other enzymes, such as phytanoyl-CoA dioxygenase. The reaction also makes IDH1 a critical contributor to the generation of NADPH, an important cofactor in many biosynthetic pathways. The cytoplasmic enzyme serves a significant role in cytoplasmic NADPH production.
The IDH1 gene encodes the NADP(+)-dependent isocitrate dehydrogenase found in the cytoplasm and peroxisomes, and the protein belongs to the isocitrate and isopropylmalate dehydrogenases family. Five isocitrate dehydrogenases have been reported in humans: three NAD(+)-dependent enzymes in the mitochondrial matrix, and two NADP(+)-dependent enzymes, one mitochondrial (IDH2) and one predominantly cytosolic (IDH1). Each NADP(+)-dependent isozyme is a homodimer. Alternatively spliced transcript variants of the gene encode the same protein.
IDH1 contains a PTS-1 peroxisomal targeting signal sequence. Its presence in peroxisomes suggests roles in regenerating NADPH for intraperoxisomal reductions, such as the conversion of 2,4-dienoyl-CoAs to 3-enoyl-CoAs, and in peroxisomal reactions that consume 2-oxoglutarate, namely the alpha-hydroxylation of phytanic acid. UniProt also notes that IDH1 may act as a corneal epithelial crystallin and may be involved in maintaining corneal epithelial transparency. Earlier HGNC names include isocitrate dehydrogenase 1 (NADP+), soluble.
IDH1 is a significant source of cytoplasmic NADPH, a cofactor required in many biosynthetic pathways.
Peroxisomal IDH1 is proposed to regenerate NADPH for intraperoxisomal reductions and supply 2-oxoglutarate for phytanic acid alpha-hydroxylation.
The enzyme generates 2-oxoglutarate, which is required by other enzymes such as phytanoyl-CoA dioxygenase.
IDH1 may act as a corneal epithelial crystallin and may help maintain corneal epithelial transparency.
IDH1 catalyses the NADP(+)-dependent oxidative decarboxylation of isocitrate to 2-oxoglutarate in the cytoplasm and peroxisomes. In doing so it generates NADPH, an important cofactor in many biosynthesis pathways, and supplies 2-oxoglutarate for enzymes such as phytanoyl-CoA dioxygenase.
Five isocitrate dehydrogenases have been reported. Three are NAD(+)-dependent and mitochondrial. Two are NADP(+)-dependent: IDH2 is mitochondrial, while IDH1 is found in the cytoplasm and peroxisomes. Each NADP(+)-dependent isozyme is a homodimer.
Yes. Mouse and rat both have an ortholog named Idh1, so the gene can be studied in common rodent models. Alternative splicing of the human gene gives transcript variants that encode the same protein. Check the datasheet of any product for its validated reactivity.
The mitochondrial NADP(+)-dependent counterpart of IDH1 and other isocitrate dehydrogenase family members with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt O75874; product specifications from Assay Genie datasheets.