内质网
生物化学
糖基转移酶
生物合成
细胞壁
酶
代谢工程
ATP合酶
聚糖
生物
化学
糖蛋白
作者
Adam Jóźwiak,Prashant Sonawane,Sayantan Panda,Constantine Garagounis,Kalliope Κ. Papadopoulou,Bekele Abebie,Hassan Massalha,Efrat Almekias-Siegl,Tali Scherf,Asaph Aharoni
标识
DOI:10.1038/s41589-020-0541-x
摘要
Glycosylation is one of the most prevalent molecular modifications in nature. Single or multiple sugars can decorate a wide range of acceptors from proteins to lipids, cell wall glycans and small molecules, dramatically affecting their activity. Here, we discovered that by 'hijacking' an enzyme of the cellulose synthesis machinery involved in cell wall assembly, plants evolved cellulose synthase-like enzymes (Csls) and acquired the capacity to glucuronidate specialized metabolites, that is, triterpenoid saponins. Apparently, endoplasmic reticulum-membrane localization of Csls and of other pathway proteins was part of evolving a new glycosyltransferase function, as plant metabolite glycosyltransferases typically act in the cytosol. Discovery of glucuronic acid transferases across several plant orders uncovered the long-pursued enzymatic reaction in the production of a low-calorie sweetener from licorice roots. Our work opens the way for engineering potent saponins through microbial fermentation and plant-based systems.
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