sesquiterpenesynthase

Sesquiterpene synthases are enzymes that catalyze the biosynthesis of sesquiterpenes, a large and structurally diverse class of organic compounds found in many plants and fungi. These enzymes are responsible for the cyclization of farnesyl pyrophosphate (FPP), a 15-carbon precursor molecule, into a wide array of sesquiterpene skeletons. The reactions involve complex carbocation rearrangements and cyclization steps, leading to the formation of hundreds of different sesquiterpene structures. The specific products formed by a sesquiterpene synthase are determined by its unique three-dimensional structure, which guides the FPP substrate through a precise reaction pathway.

These enzymes play crucial roles in plant defense mechanisms, acting as a source of volatile compounds that can repel herbivores or attract predators of those herbivores. They are also involved in plant-insect communication. In some organisms, sesquiterpenes synthesized by these enzymes have pharmacological properties, leading to research into their potential medicinal applications, such as anti-inflammatory or anti-cancer agents. The study of sesquiterpene synthases is an active area of research in biochemistry and natural product chemistry, aiming to understand their catalytic mechanisms, discover new sesquiterpene structures, and harness their biosynthetic potential for various applications.