Identification of a diarylpentanoid-producing polyketide synthase revealing an unusual biosynthetic pathway of 2-(2-phenylethyl)chromones in agarwood

Xiao-Hui Wang, Bo-Wen Gao, Yu Nakashima, Takahiro Mori, Zhong-Xiu Zhang, Takeshi Kodama, Yuan-E Lee, Ze-Kun Zhang, Chin-Piow Wong, Qian-Qian Liu, Bo-Wen Qi, Juan Wang, Jun Li, Xiao Liu, Ikuro Abe, Hiroyuki Morita (), Peng-Fei Tu () and She-Po Shi ()
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Xiao-Hui Wang: Beijing University of Chinese Medicine
Bo-Wen Gao: Beijing University of Chinese Medicine
Yu Nakashima: University of Toyama
Takahiro Mori: The University of Tokyo
Zhong-Xiu Zhang: Beijing University of Chinese Medicine
Takeshi Kodama: University of Toyama
Yuan-E Lee: University of Toyama
Ze-Kun Zhang: Beijing University of Chinese Medicine
Chin-Piow Wong: University of Toyama
Qian-Qian Liu: University of Toyama
Bo-Wen Qi: Beijing University of Chinese Medicine
Juan Wang: Beijing University of Chinese Medicine
Jun Li: Beijing University of Chinese Medicine
Xiao Liu: Beijing University of Chinese Medicine
Ikuro Abe: The University of Tokyo
Hiroyuki Morita: University of Toyama
Peng-Fei Tu: Beijing University of Chinese Medicine
She-Po Shi: Beijing University of Chinese Medicine

Nature Communications, 2022, vol. 13, issue 1, 1-12

Abstract: Abstract 2-(2-Phenylethyl)chromones (PECs) are the principal constituents contributing to the distinctive fragrance of agarwood. How PECs are biosynthesized is currently unknown. In this work, we describe a diarylpentanoid-producing polyketide synthase (PECPS) identified from Aquilaria sinensis. Through biotransformation experiments using fluorine-labeled substrate, transient expression of PECPS in Nicotiana benthamiana, and knockdown of PECPS expression in A. sinensis calli, we demonstrate that the C6–C5–C6 scaffold of diarylpentanoid is the common precursor of PECs, and PECPS plays a crucial role in PECs biosynthesis. Crystal structure (1.98 Å) analyses and site-directed mutagenesis reveal that, due to its small active site cavity (247 Å3), PECPS employs a one-pot formation mechanism including a “diketide-CoA intermediate-released” step for the formation of the C6–C5–C6 scaffold. The identification of PECPS, the pivotal enzyme of PECs biosynthesis, provides insight into not only the feasibility of overproduction of pharmaceutically important PECs using metabolic engineering approaches, but also further exploration of how agarwood is formed.

Date: 2022
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DOI: 10.1038/s41467-022-27971-z

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