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Delta-5-desaturase is an iron-containing enzyme encoded by the FADS1 gene in humans. It catalyzes a key step in polyunsaturated fatty acid biosynthesis by introducing a double bond at carbon 5 from the carboxyl end—specifically converting dihomo-gamma-linolenic acid (20:3 n−6) into arachidonic acid (20:4 n−6), and eicosatetraenoic acid into eicosapentaenoic acid (EPA). These products are critical precursors for bioactive lipid mediators involved in cell signaling, membrane fluidity regulation, and inflammatory responses. Genetic variants affecting FADS1 activity have been strongly linked to cardiometabolic diseases such as obesity, diabetes mellitus type 2, dyslipidemia, nonalcoholic fatty liver disease, elevated liver enzymes, and coronary artery disease. The enzyme is considered a promising therapeutic target due to its central role in regulating both pro-inflammatory and anti-inflammatory lipid mediator synthesis.[1][2][3][4]
Drugs that inhibit Delta-5-desaturase block the conversion of dihomo-gamma-linolenic acid (DGLA) to arachidonic acid. This reduces levels of pro-inflammatory eicosanoids derived from arachidonic acid and may modulate inflammation and metabolic processes[2][5].
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