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Multiple dehydrogenases and oxidoreductases refer to a broad category of enzymes (EC 1) that facilitate the transfer of electrons between molecules, a process fundamental to cellular life [1]. These enzymes, which include subclasses like dehydrogenases, oxidases, and reductases, are central to energy production in the mitochondria and the metabolism of carbohydrates, lipids, and amino acids [4]. In a therapeutic context, this term often describes the multi-target profile of certain drugs, such as disulfiram, which inhibits several enzymes including aldehyde dehydrogenase and potentially other thiol-dependent oxidoreductases [2]. Targeting these enzymes is a strategy used in treating alcohol dependence and is being explored in oncology to disrupt the metabolic flexibility of cancer cells [3]. Because these enzymes are ubiquitous and essential for homeostasis, pharmacological intervention requires careful management to avoid systemic toxicity and severe drug-alcohol interactions [2, 4]. They play a vital role in maintaining the redox balance of the cell, and their dysfunction is linked to various metabolic and neurodegenerative diseases [4]. Overall, while not a single protein, this group represents a critical node in metabolic regulation and drug development [1, 3].
Inhibition of enzymatic activity through various mechanisms, including covalent modification of active-site cysteine residues or competition with cofactors like NAD+/NADH [2, 4].
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