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X-ray Structural Study on Polyketide Synthase Involved in Olivetolic Acid Biosynthesis in Cannabis sativa

https://repo.qst.go.jp/records/80212
https://repo.qst.go.jp/records/80212
0d2bbe6c-8e37-40e9-92fa-a85d4b198b75
Item type 会議発表用資料 / Presentation(1)
公開日 2020-07-16
タイトル
タイトル X-ray Structural Study on Polyketide Synthase Involved in Olivetolic Acid Biosynthesis in Cannabis sativa
言語
言語 eng
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_c94f
資源タイプ conference object
アクセス権
アクセス権 metadata only access
アクセス権URI http://purl.org/coar/access_right/c_14cb
著者 Kono, Fumiaki

× Kono, Fumiaki

WEKO 878466

Kono, Fumiaki

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Taguchi, Chiho

× Taguchi, Chiho

WEKO 878467

Taguchi, Chiho

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Blaber, Michael

× Blaber, Michael

WEKO 878468

Blaber, Michael

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Kuroki, Ryota

× Kuroki, Ryota

WEKO 878469

Kuroki, Ryota

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Morimoto, Satoshi

× Morimoto, Satoshi

WEKO 878470

Morimoto, Satoshi

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Tamada, Taro

× Tamada, Taro

WEKO 878471

Tamada, Taro

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Kono, Fumiaki

× Kono, Fumiaki

WEKO 878472

en Kono, Fumiaki

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Tamada, Taro

× Tamada, Taro

WEKO 878473

en Tamada, Taro

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抄録
内容記述タイプ Abstract
内容記述 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.
会議概要(会議名, 開催地, 会期, 主催者等)
内容記述タイプ Other
内容記述 第20回日本蛋白質科学会年会
発表年月日
日付 2020-07-15
日付タイプ Issued
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