聚酮合酶
生物合成
查尔酮合酶
生物化学
柚皮素
腺苷酸化
聚酮
生物
蓝蛋白
酰基转移酶
酶
丙炔基转移酶
化学
立体化学
类黄酮
抗氧化剂
脂肪酸合酶
作者
Hongjiao Zhang,Zixin Li,Shuling Zhou,Shu‐Ming Li,Huomiao Ran,Zili Song,Tao Yu,Wen‐Bing Yin
标识
DOI:10.1038/s41467-022-34150-7
摘要
Biosynthesis of the flavonoid naringenin in plants and bacteria is commonly catalysed by a type III polyketide synthase (PKS) using one p-coumaroyl-CoA and three malonyl-CoA molecules as substrates. Here, we report a fungal non-ribosomal peptide synthetase -polyketide synthase (NRPS-PKS) hybrid FnsA for the naringenin formation. Feeding experiments with isotope-labelled precursors demonstrate that FnsA accepts not only p-coumaric acid (p-CA), but also p-hydroxybenzoic acid (p-HBA) as starter units, with three or four malonyl-CoA molecules for elongation, respectively. In vitro assays and MS/MS analysis prove that both p-CA and p-HBA are firstly activated by the adenylation domain of FnsA. Phylogenetic analysis reveals that the PKS portion of FnsA shares high sequence homology with type I PKSs. Refactoring the biosynthetic pathway in yeast with the involvement of fnsA provides an alternative approach for the production of flavonoids such as isorhamnetin and acacetin.
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