@misc{oai:repo.qst.go.jp:00080212,
 author = {Kono, Fumiaki and Taguchi, Chiho and Blaber, Michael and Kuroki, Ryota and Morimoto, Satoshi and Tamada, Taro and Kono, Fumiaki and Tamada, Taro},
 month = {Jul},
 note = {Cannabis sativa L. produces unique secondary metabolites known as cannabinoids which have psychotropic and pharmacological activities. Major cannabinoids including DELTA9-tetrahydrocannabinol are biosynthesized from a common precursor olivetolic acid. A type III polyketide synthetase (PKS) from C. sativa named PKS-1 is considered to synthesize the tetraketide intermediate of olivetolic acid by condensation of hexanoyl-CoA with three malonyl-CoA molecules. Whereas most plant PKSs can react with various CoA esters, PKS-1 exhibits a relatively strict substrate specificity for hexanoyl-CoA as the starter substrate. The unique enzymatic property of PKS-1 is important in the cannabinoid pathway. To clarify the structure-function relationship of PKS-1, we have determined X-ray crystal structures of recombinant apo PKS-1 and complexes with hexanoyl-CoA or malonyl-CoA, at resolutions of 1.6 Å, 1.6 Å and 1.8 Å, respectively. The overall structure of PKS-1 is similar to those of other plant PKSs. As for the loop regions around the active site of PKS-1, which are thought to characterize the enzymatic properties, their structures are most similar to those of pyrone synthase from Gerbera hybrida. The binding pattern of the CoA moiety to PKS-1 is similar between hexanoyl-CoA and malonyl-CoA. Compared to other plant PKSs, several amino acid side chains of PKS-1 that constitute the active site cavity are positioned to effectively reduce the cavity volume and bind the aliphatic moiety of hexanoyl-CoA tightly. These structural features of PKS-1 are considered to enable selective binding of hexanoyl-CoA leading to production of cannabinoids unique to C. sativa., 第20回日本蛋白質科学会年会},
 title = {X-ray Structural Study on Polyketide Synthase Involved in Olivetolic Acid Biosynthesis in Cannabis sativa},
 year = {2020}
}