The selective formation of E- or Z-isomers is an important process in natural product metabolism. We show that the subunit composition of an enzyme can alter the geometrical composition of the enzymatic products. Hinokiresinol synthase, purified from Asparagus officinalis cell cultures, is responsible for the conversion of (7E,7'E)-4-coumaryl 4-coumarate to (Z)-hinokiresinol, the first step in norlignan formation. The protein is most likely a heterodimer composed of two distinct subunits, which share identity with members of the phloem protein 2 gene superfamily. Interestingly, each recombinant subunit of hinokiresinol synthase expressed in Escherichia coli solely converted (7E,7'E)-4-coumaryl 4-coumarate to the unnatural (E)-hinokiresinol, the E-isomer of (Z)-hinokiresinol. By contrast, a mixture of recombinant subunits catalyzed the formation of (Z)-hinokiresinol from the same substrate.
The subunit composition of hinokiresinol synthase controls geometrical selectivity in norlignan formation. Publishing Authors By Initials
The subunit composition of hinokiresinol synthase controls geometrical selectivity in norlignan formation. Journal Published:
PUBLICATION TYPE: Journal Article
Journal: Proceedings of the National Academy of Sciences of
VOLUME: 104
Page Numbers: 21008-13
Journal Abbreviation: Proc. Natl. Acad. Sci. U.S.A.
ISSN: 1091-6490
DAY: 19
MONTH: 12
YEAR: 2007
The subunit composition of hinokiresinol synthase controls geometrical selectivity in norlignan formation. Information
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LANGUAGE: eng
NlmUniqueID: 7505876
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Grant and Affiliation Information for The subunit composition of hinokiresinol synthase controls geometrical selectivity in norlignan formation.
AFFILIATION: Research Institute for Sustainable Humanosphere and Institute of Sustainability Science, Kyoto University, Uji, Kyoto 611-0011, Japan.
Country: United States
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MEDLINETA: Proc Natl Acad Sci U S A
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