In enzymology, bornyl diphosphate synthase (BPPS) (EC 5.5.1.8) is an enzyme that catalyzes the chemical reaction
Bornyl diphosphate synthase is involved in the biosynthesis of the cyclic monoterpenoid bornyl diphosphate. As seen from the reaction above, BPPS takes geranyl diphosphate as its only substrate and isomerizes into the product, (+)- bornyl diphosphate. This reaction comes from a general class of enzymes called terpene synthases that cyclize a universal precursor, geranyl diphosphate, to form varying monocyclic and bicyclic monoterpenes. The biochemical transformation of geranyl diphosphate to cyclic products occurs in a variety of aromatic plants, including both angiosperms and gymnosperms, and is used for various purposes described in sections below. Terpene synthases like BPPS are the primary enzymes in the formation of low-molecular-weight terpene metabolites. The organization of terpene synthases, their characteristic ability to form multiple products, and regulation in response to biotic and abiotic factors contribute to the formation of a diverse group of terpene metabolites. The structural diversity and complexity of terpenes generates an enormous potential for mediating plant–environment interactions.
The systematic name of this enzyme class is (+)-bornyl-diphosphate lyase (decyclizing). Other names in common use include bornyl pyrophosphate synthase, bornyl pyrophosphate synthetase, (+)-bornylpyrophosphate cyclase, and geranyl-diphosphate cyclase (ambiguous). This enzyme participates in monoterpenoid biosynthesis and belongs to the family of isomerases, specifically the class of intramolecular lyases.
The chirality of borneol in a plant depends on the preferred chirality of the bornyl diphosphate synthase. Synthases for either chirality have been sequenced: this article deals with the better-characterized (+)-bornyl diphosphate synthase. In 2021, scientists discovered the first known (-)-bornyl diphosphate synthase.