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Dehydrogenases are enzymes that catalyze oxidation-reduction reactions, specifically the removal of hydrogen atoms from a particular substrate. This process typically involves the transfer of hydrogen atoms to a coenzyme, such as NAD+ (nicotinamide adenine dinucleotide) or NADP+ (nicotinamide adenine dinucleotide phosphate), which is then reduced to NADH or NADPH, respectively. These coenzymes act as electron carriers, facilitating the transfer of electrons and protons within metabolic pathways.

Dehydrogenases play crucial roles in a wide variety of biological processes. They are essential for energy metabolism, including glycolysis, the citric acid cycle, and oxidative phosphorylation, where they are involved in the breakdown of glucose and other fuel molecules to produce ATP. They are also important in the biosynthesis of various compounds, such as fatty acids and steroids, and in the detoxification of harmful substances.

The activity of dehydrogenases is often regulated by the availability of their substrates and coenzymes, as well as by allosteric effectors. Many dehydrogenases are also subject to regulation at the transcriptional and translational levels. Dysfunctional dehydrogenases can lead to a range of metabolic disorders, highlighting their critical importance in maintaining cellular homeostasis. Examples of specific dehydrogenases include lactate dehydrogenase, which converts lactate to pyruvate, and alcohol dehydrogenase, which oxidizes ethanol.