Enzyme cofactor function

Enzyme cofactor functions describe the indispensable roles that non-protein molecules—called cofactors—play in enabling enzymes to catalyze biochemical reactions essential for life[1][2][4][5][6][7]. Cofactors can be either **inorganic (metal ions such as zinc, iron, or copper)** or **organic (coenzymes, usually vitamin-derived molecules such as NAD⁺, FAD, coenzyme A, etc.)**[1][2][4][5][6][7]. They help stabilize the enzyme’s structure, facilitate binding to substrates, or participate directly in the chemical reactions catalyzed by the enzyme[1][2][4][5][6][7]. Some cofactors are transiently associated with enzymes (cosubstrates) and are modified during catalysis, while others (prosthetic groups) are tightly or permanently bound[1][2][4][5][6][7]. The absence of the required cofactor often renders the enzyme inactive (apoenzyme), whereas the enzyme-cofactor complex is termed a holoenzyme[1][2][4][5][7]. Each enzyme-cofactor system is unique and can play roles in energy transfer, redox reactions, group transfer, or stabilization of charged reaction intermediates[1][2][4][5][7]. The function is central to all of biochemistry but is not a discrete molecular entity or drug target.

Other names

Cofactor functionCofactor activityCofactor-mediated catalysisEnzyme cofactor roles