A fungal NRPS-PKS enzyme catalyses the formation of the flavonoid naringenin

Hongjiao Zhang, Zixin Li, Shuang Zhou, Shu-Ming Li, Huomiao Ran, Zili Song, Tao Yu and Wen-Bing Yin ()
Additional contact information
Hongjiao Zhang: Chinese Academy of Sciences
Zixin Li: Chinese Academy of Sciences
Shuang Zhou: Chinese Academy of Sciences
Shu-Ming Li: Philipps-Universität Marburg
Huomiao Ran: Chinese Academy of Sciences
Zili Song: Chinese Academy of Sciences
Tao Yu: Chinese Academy of Sciences
Wen-Bing Yin: Chinese Academy of Sciences

Nature Communications, 2022, vol. 13, issue 1, 1-11

Abstract: Abstract 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.

Date: 2022
References: View references in EconPapers View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-022-34150-7 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-34150-7

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-022-34150-7

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().