dehidrogenaz

Dehidrogenaz, or dehydrogenases, are enzymes that catalyze oxidation–reduction reactions in which hydrogen atoms are removed from substrates. In most cases, the electrons from the substrate are transferred to a catalytic cofactor such as NAD+, NADP+, or FAD, which becomes reduced and then passes the electrons to an electron acceptor in metabolism. Dehidrogenaz form a large and diverse family within the oxidoreductases (EC 1), with members classified by the substrate they act on or by cofactor preference.

Common examples include lactate dehidrogenaz (LDH), malate dehidrogenaz (MDH), glyceraldehyde-3-phosphate dehidrogenaz (GAPDH), and alcohol dehidrogenaz. Some dehidrogenaz, such as succinate dehidrogenaz, are components of the mitochondrial electron transport chain and connect the tricarboxylic acid cycle to respiration. Mechanistically, many dehidrogenaz remove a hydride from the substrate and transfer it to a bound cofactor. Structural features often include a Rossmann fold for nucleotide binding, though some enzymes use metal ions or FAD as prosthetic groups.

Locations within the cell vary, including cytosol and mitochondria, reflecting roles in energy metabolism, redox balance, and biosynthetic pathways. Clinically, altered dehidrogenaz activity can serve as a biomarker (for example, LDH isoforms in tissue damage). In industry, these enzymes are exploited as biocatalysts for stereoselective synthesis and for regenerating NADH in biotechnological processes.