| Cannabidiolic acid synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.21.3.8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDBPDBePDBsum | ||||||||
| |||||||||
Cannabidiolic acid synthase (EC1.21.3.8,CBDA synthase) is anenzyme withsystematic namecannabigerolate:oxygen oxidoreductase (cyclizing, cannabidiolate-forming).[1][2] It is anoxidoreductase found inCannabis sativa that catalyses the formation ofcannabidiolate, acarboxylatedprecursor ofcannabidiol.[2]
Cannabidiolic acid synthase consists of a single protein with a molecular mass of 74 kDa.[1] Its amino acid sequence is partly (40-50%) homologous to several other oxidoreductases,[2] such asberberine bridge enzyme inEschscholzia californica[3] andNectarin V inNicotiana langsdorffii X N. sanderae.[4]
CBDA synthase has four binding sites; two forFAD and two for the substrate.[5]
Cannabidiolic acid synthasecatalyses the production ofcannabidiolate predominantly fromcannabigerolate by stereospecific oxidative cyclization of thegeranyl group ofcannabigerolic acid[2] according to the followingchemical reaction:
Cannabinerolate can also be used as a substrate, but with lower efficiency (KM=0.137 mM) thancannabigerolate (KM=0.206 mM). Itcovalently binds FAD, and does require coenzymes & molecular oxygen for the oxidocyclization reaction.[1]
The optimum pH for CBDA synthase is 5.0.[2]
