A serine carboxypeptidase-like acyltransferase catalyzes consecutive four-step reactions of hydrolyzable tannin biosynthesis in Camellia oleifera.

Autor: Wang Z; State Key Laboratory of Tea Plant Biology and Utilization/Key Laboratory of Tea Biology and Tea Processing of Ministry of Agriculture/Anhui Provincial Laboratory of Tea Plant Biology and Utilization, Anhui Agricultural University, Hefei, China.; Core Facility Center, Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology, Shanghai, China., Chen X; School of Life Science, Anhui Agricultural University, Hefei, China., Zhao Y; State Key Laboratory of Tea Plant Biology and Utilization/Key Laboratory of Tea Biology and Tea Processing of Ministry of Agriculture/Anhui Provincial Laboratory of Tea Plant Biology and Utilization, Anhui Agricultural University, Hefei, China., Jin D; School of Life Science, Anhui Agricultural University, Hefei, China., Jiang C; School of Life Science, Anhui Agricultural University, Hefei, China., Yao S; State Key Laboratory of Tea Plant Biology and Utilization/Key Laboratory of Tea Biology and Tea Processing of Ministry of Agriculture/Anhui Provincial Laboratory of Tea Plant Biology and Utilization, Anhui Agricultural University, Hefei, China., Li Z; School of Life Science, Anhui Agricultural University, Hefei, China., Jiang X; State Key Laboratory of Tea Plant Biology and Utilization/Key Laboratory of Tea Biology and Tea Processing of Ministry of Agriculture/Anhui Provincial Laboratory of Tea Plant Biology and Utilization, Anhui Agricultural University, Hefei, China., Liu Y; State Key Laboratory of Tea Plant Biology and Utilization/Key Laboratory of Tea Biology and Tea Processing of Ministry of Agriculture/Anhui Provincial Laboratory of Tea Plant Biology and Utilization, Anhui Agricultural University, Hefei, China.; School of Life Science, Anhui Agricultural University, Hefei, China., Gao L; State Key Laboratory of Tea Plant Biology and Utilization/Key Laboratory of Tea Biology and Tea Processing of Ministry of Agriculture/Anhui Provincial Laboratory of Tea Plant Biology and Utilization, Anhui Agricultural University, Hefei, China.; School of Life Science, Anhui Agricultural University, Hefei, China., Xia T; State Key Laboratory of Tea Plant Biology and Utilization/Key Laboratory of Tea Biology and Tea Processing of Ministry of Agriculture/Anhui Provincial Laboratory of Tea Plant Biology and Utilization, Anhui Agricultural University, Hefei, China.
Jazyk: angličtina
Zdroj: The Plant journal : for cell and molecular biology [Plant J] 2024 Aug; Vol. 119 (3), pp. 1299-1312. Date of Electronic Publication: 2024 Jun 05.
DOI: 10.1111/tpj.16849
Abstrakt: Hydrolyzable tannins (HTs), a class of polyphenolic compounds found in dicotyledonous plants, are widely used in food and pharmaceutical industries because of their beneficial effects on human health. Although the biosynthesis of simple HTs has been verified at the enzymatic level, relevant genes have not yet been identified. Here, based on the parent ion-fragment ion pairs in the feature fragment data obtained using UPLC-Q-TOF-/MS/MS, galloyl phenolic compounds in the leaves of Camellia sinensis and C. oleifera were analyzed qualitatively and quantitatively. Correlation analysis between the transcript abundance of serine carboxypeptidase-like acyltransferases (SCPL-ATs) and the peak area of galloyl products in Camellia species showed that SCPL3 expression was highly correlated with HT biosynthesis. Enzymatic verification of the recombinant protein showed that CoSCPL3 from C. oleifera catalyzed the four consecutive steps involved in the conversion of digalloylglucose to pentagalloylglucose. We also identified the residues affecting the enzymatic activity of CoSCPL3 and determined that SCPL-AT catalyzes the synthesis of galloyl glycosides. The findings of this study provide a target gene for germplasm innovation of important cash crops that are rich in HTs, such as C. oleifera, strawberry, and walnut.
(© 2024 Society for Experimental Biology and John Wiley & Sons Ltd.)
Databáze: MEDLINE
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