cannabigerolic-acid and cannabidiolic-acid

As a complement to vaccines, small-molecule therapeutic agents are needed to treat or prevent infections by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) and its variants, which cause COVID-19. Affinity selection-mass spectrometry was used for the discovery of botanical ligands to the SARS-CoV-2 spike protein. Cannabinoid acids from hemp (

Topics: Angiotensin-Converting Enzyme 2; Animals; Antiviral Agents; Benzoates; Cannabinoids; Chlorocebus aethiops; COVID-19; COVID-19 Drug Treatment; Humans; Ligands; Mass Spectrometry; Models, Molecular; Protein Binding; SARS-CoV-2; Spike Glycoprotein, Coronavirus; Vero Cells; Virus Internalization

The regulation of cannabinoid synthesis in

Topics: Benzoates; Cannabinoids; Cannabis; Dronabinol; Intramolecular Oxidoreductases; Plant Breeding; Plant Proteins; Polymorphism, Single Nucleotide

Topics: Animals; Anticonvulsants; Brain; Cannabinoids; Epilepsies, Myoclonic; Epilepsy, Tonic-Clonic; Female; Half-Life; Injections, Intraperitoneal; Male; Mice; Mice, Inbred C57BL; Mice, Knockout; NAV1.1 Voltage-Gated Sodium Channel

Cannabis sativa L. has been cultivated and used around the globe for its medicinal properties for millennia

Topics: Acyl Coenzyme A; Alkyl and Aryl Transferases; Benzoates; Biosynthetic Pathways; Cannabinoids; Cannabis; Dronabinol; Fermentation; Galactose; Metabolic Engineering; Mevalonic Acid; Polyisoprenyl Phosphates; Saccharomyces cerevisiae; Salicylates

Cannabinoids are secondary natural products from the plant Cannabis sativaL. Therapeutic indications of cannabinoids currently comprise a significant area of medicinal research. We have expressed the Δ

Topics: Benzoates; Cannabinoids; Cannabis; Catalysis; Catalytic Domain; Dronabinol; Glycolysis; Hydrogen-Ion Concentration; Intramolecular Oxidoreductases; Plant Proteins; Recombinant Proteins; Saccharomycetales; Structure-Activity Relationship; Temperature

We identified a unique enzyme that catalyzes the oxidocyclization of cannabigerolic acid to cannabidiolic acid (CBDA) in Cannabis sativa L. (CBDA strain). The enzyme, named CBDA synthase, was purified to apparent homogeneity by a four-step procedure: ammonium sulfate precipitation followed by chromatography on DEAE-cellulose, phenyl-Sepharose CL-4B, and hydroxylapatite. The active enzyme consists of a single polypeptide with a molecular mass of 74 kDa and a pI of 6.1. The NH2-terminal amino acid sequence of CBDA synthase is similar to that of Delta1-tetrahydrocannabinolic-acid synthase. CBDA synthase does not require coenzymes, molecular oxygen, hydrogen peroxide, and metal ion cofactors for the oxidocyclization reaction. These results indicate that CBDA synthase is neither an oxygenase nor a peroxidase and that the enzymatic cyclization does not proceed via oxygenated intermediates. CBDA synthase catalyzes the formation of CBDA from cannabinerolic acid as well as cannabigerolic acid, although the kcat for the former (0.03 s-1) is lower than that for the latter (0.19 s-1). Therefore, we conclude that CBDA is predominantly biosynthesized from cannabigerolic acid rather than cannabinerolic acid.

Topics: Amino Acid Sequence; Benzoates; Cannabinoids; Cannabis; Chromatography; Chromatography, High Pressure Liquid; Chromatography, Ion Exchange; Durapatite; Electrophoresis, Polyacrylamide Gel; Intramolecular Oxidoreductases; Isomerases; Kinetics; Molecular Sequence Data; Molecular Structure; Molecular Weight; Peptide Fragments; Plant Leaves; Sequence Homology, Amino Acid; Species Specificity; Substrate Specificity