redutase

Redutase is not a standard term in biochemical nomenclature. When encountered, it is usually a misspelling or variant of reductase, a broad class of enzymes that catalyze reduction reactions. In general, reductases transfer electrons to a substrate, often using cofactors such as NADH or NADPH as electron donors. Some reductases also employ flavin cofactors (FAD or FMN) or iron-sulfur clusters to mediate electron transfer.

Reductases are classified within the enzyme commission system as oxidoreductases (EC 1), specifically those that reduce another molecule. They participate in diverse biological processes, including metabolism, detoxification, and biosynthesis. Many reductases catalyze the addition of hydrogen or the transfer of electrons to carbon, nitrogen, or oxygen atoms, thereby altering a substrate’s oxidation state and reactivity. The direction and outcome of the reaction can depend on cellular conditions, cofactor availability, and substrate concentration.

Several well-studied subfamilies illustrate the diversity of reductases. Aldo-keto reductases reduce carbonyl groups in sugars, steroids, and other metabolites. Nitroreductases and azoreductases participate in xenobiotic metabolism and the breakdown of nitro compounds. Old yellow enzyme family members are flavin-dependent reductases involved in various redox reactions. In biotechnology, microbial reductases are exploited for asymmetric synthesis, drug metabolism studies, and bioremediation.

If encountering the term redutase in literature, it is advisable to verify the intended spelling and context, as it most often points to reductase activity rather than a distinct enzyme name.