A fungal NRPS-PKS enzyme catalyses the formation of the flavonoid naringenin
説明
<jats:title>Abstract</jats:title><jats:p>Biosynthesis of the flavonoid naringenin in plants and bacteria is commonly catalysed by a type III polyketide synthase (PKS) using one<jats:italic>p</jats:italic>-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<jats:italic>p</jats:italic>-coumaric acid (<jats:italic>p</jats:italic>-CA), but also<jats:italic>p</jats:italic>-hydroxybenzoic acid (<jats:italic>p</jats:italic>-HBA) as starter units, with three or four malonyl-CoA molecules for elongation, respectively. In vitro assays and MS/MS analysis prove that both<jats:italic>p</jats:italic>-CA and<jats:italic>p</jats:italic>-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<jats:italic>fnsA</jats:italic>provides an alternative approach for the production of flavonoids such as isorhamnetin and acacetin.</jats:p>
収録刊行物
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- Nature Communications
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Nature Communications 13 (1), 6361-, 2022-10-26
Springer Science and Business Media LLC
