dehidrogenases

Dehydrogenases are a class of enzymes that catalyze oxidation-reduction reactions, specifically the removal of hydrogen atoms from a substrate. These reactions are crucial for a wide range of metabolic processes in living organisms, including cellular respiration, photosynthesis, and the synthesis and breakdown of various biomolecules. Dehydrogenases typically utilize coenzymes, such as NAD+ (nicotinamide adenine dinucleotide) or NADP+ (nicotinamide adenine dinucleotide phosphate), to accept the hydrogen atoms and electrons removed from the substrate. In the process, NAD+ is reduced to NADH, and NADP+ is reduced to NADPH, which then often go on to participate in other enzymatic reactions, carrying energy or reducing power.

The substrate specificity of dehydrogenases is quite high, meaning each enzyme typically acts on a particular molecule or a closely related group of molecules. This specificity ensures that metabolic pathways proceed in a controlled and efficient manner. Examples of important dehydrogenases include lactate dehydrogenase, which interconverts lactate and pyruvate, and glucose-6-phosphate dehydrogenase, a key enzyme in the pentose phosphate pathway. Dehydrogenases are also widely studied and utilized in biotechnology and medicine, for instance, in diagnostic tests and in the development of therapeutic agents. Their role in facilitating energy transfer and biochemical transformations makes them indispensable components of life's chemistry.