Dehydrogenase enzyme

A **dehydrogenase enzyme** is a member of the oxidoreductase family (EC class 1), catalyzing the removal of hydrogen atoms from substrates in oxidation-reduction reactions[1][3][6][8]. Typically, dehydrogenases use coenzymes such as NAD+, NADP+, FAD, or FMN as electron acceptors, facilitating essential steps in major metabolic pathways including glycolysis, the citric acid cycle, fatty acid oxidation, and amino acid catabolism[1][3][4][8]. The term "dehydrogenase enzyme" is generic and refers to a large group of distinct enzymes (such as alcohol dehydrogenase, lactate dehydrogenase, pyruvate dehydrogenase, aldehyde dehydrogenase, etc.), each with specific substrates and biological roles[3][7][1]. Dysregulation or mutation of individual dehydrogenases is associated with diseases including certain cancers, metabolic disorders, cardiovascular and neurological diseases[1][2]. Certain dehydrogenases can serve as biomarkers (e.g., elevated serum LDH as a marker of tissue damage or tumor activity, ALDH activity for some cancer stem cells)[1][2]. Many drugs act by targeting specific dehydrogenases (e.g., disulfiram inhibits aldehyde dehydrogenase for alcohol aversion therapy; metformin inhibits mitochondrial glycerol-3-phosphate dehydrogenase for diabetes management; brequinar targets dihydroorotate dehydrogenase in cancer)[1][8]. Because "dehydrogenase enzyme" is a non-specific, collective term rather than a single defined molecular target, information may need to be refined to a specific isoform or family member for actionable therapeutic or research use[3].

Other names

DehydrogenaseOxidoreductase (when appropriate)e.g. "Alcohol dehydrogenase,""Lactate dehydrogenase," etc.

Enzyme inhibition, Enzyme activation, Modulation of metabolic flux