Isocitrate dehydrogenase (IDH) (EC 1.1.1.42) and (EC 1.1.1.41) is an enzyme that catalyzes the oxidative decarboxylation of isocitrate, producing alpha-ketoglutarate (α-ketoglutarate) and CO2. This is a two-step process, which involves oxidation of isocitrate (a secondary alcohol) to oxalosuccinate (a ketone), followed by the decarboxylation of the carboxyl group beta to the ketone, forming alpha-ketoglutarate. In humans, IDH exists in three isoforms: IDH3 catalyzes the third step of the citric acid cycle while converting NAD+ to NADH in the mitochondria. The isoforms IDH1 and IDH2 catalyze the same reaction outside the context of the citric acid cycle and use NADP+ as a cofactor instead of NAD+. They localize to the cytosol as well as the mitochondrion and peroxisome.
2-hydroxyglutaric aciduria is a rare neurometabolic disorder characterized by the significantly elevated levels of hydroxyglutaric acid in one's urine. It is either autosomal recessive or autosomal dominant.
In enzymology, a 4-hydroxybutyrate dehydrogenase (EC 1.1.1.61) is an enzyme that catalyzes the chemical reaction
In enzymology, 3-hydroxybutyrate dehydrogenase (EC 1.1.1.30) is an enzyme that catalyzes the chemical reaction:
In enzymology, a (R)-2-hydroxyacid dehydrogenase (EC 1.1.1.272) is an enzyme that catalyzes the chemical reaction
In enzymology, a 2'-deoxymugineic-acid 2'-dioxygenase (EC 1.14.11.24) is an enzyme that catalyzes the chemical reaction
In enzymology, an L-2-hydroxyglutarate dehydrogenase is an enzyme that catalyzes the chemical reaction
In enzymology, an (S)-2-hydroxy-acid oxidase (EC 1.1.3.15) is an enzyme that catalyzes the chemical reaction
In enzymology, a 3-oxoacid CoA-transferase is an enzyme that catalyzes the chemical reaction
The enzyme 4-hydroxy-2-oxoglutarate aldolase catalyzes the chemical reaction
In enzymology, a 2-hydroxyglutarate synthase (EC 2.3.3.11) is an enzyme that catalyzes the chemical reaction
Phosphoglycerate dehydrogenase (PHGDH) is an enzyme that catalyzes the chemical reactions
D-2-hydroxyglutarate dehydrogenase, mitochondrial is an enzyme that in humans is encoded by the D2HGDH gene.
L-2-hydroxyglutarate dehydrogenase, mitochondrial is an enzyme that in humans is encoded by the L2HGDH gene, also known as C14orf160, on chromosome 14.
α-Hydroxyglutaric acid is an alpha hydroxy acid form of glutaric acid.
L-2-hydroxycarboxylate dehydrogenase (NAD+) (EC 1.1.1.337, (R)-sulfolactate:NAD+ oxidoreductase, L-sulfolactate dehydrogenase, (R)-sulfolactate dehydrogenase, L-2-hydroxyacid dehydrogenase (NAD+), ComC) is an enzyme with systematic name (2S)-2-hydroxycarboxylate:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction
In enzymology, a D-2-hydroxyglutarate dehydrogenase is an enzyme that catalyzes the chemical reaction
Metabolite damage can occur through enzyme promiscuity or spontaneous chemical reactions. Many metabolites are chemically reactive and unstable and can react with other cell components or undergo unwanted modifications. Enzymatically or chemically damaged metabolites are always useless and often toxic. To prevent toxicity that can occur from the accumulation of damaged metabolites, organisms have damage-control systems that:
- Reconvert damaged metabolites to their original, undamaged form
- Convert a potentially harmful metabolite to a benign one
- Prevent damage from happening by limiting the build-up of reactive, but non-damaged metabolites that can lead to harmful products
Alcohol dehydrogenase, iron containing 1 is a protein that in humans is encoded by the ADHFE1 gene.
Coenzyme A transferases (CoA-transferases) are transferase enzymes that catalyze the transfer of a coenzyme A group from an acyl-CoA donor to a carboxylic acid acceptor. Among other roles, they are responsible for transfer of CoA groups during fermentation and metabolism of ketone bodies. These enzymes are found in all three domains of life.
