Functional specialization of two UDP‐glycosyltransferases MpUGT735A2 and MpUGT743A1 in the liverworts Marchantia polymorpha

Family 1 UDP‐glycosyltransferases (UGTs) are known to glycosylate multiple secondary plant metabolites and have been extensively studied. The increased availability of plant genome resources allows the identification of wide gene families, both functional and organizational. In this investigation, t...

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Published in:Journal of cellular physiology 2023-10, Vol.238 (10), p.2499-2511
Main Authors: Zhu, Ting‐Ting, Ta, He, Ni, Rong, Hao, Yue, Du, Ni‐Hong, Cheng, Ai‐Xia, Lou, Hong‐Xiang
Format: Article
Language:English
Subjects:
Biocatalysts
Biomedical materials
Catalysis
Enzymatic activity
Flavones
Flavonoids
Flavonols
Gene families
Genomes
Glycosylation
Isoflavones
Isoforms
Kaempferol
Marchantiophyta
Metabolites
Mutagenesis
Phenylpropanoids
Regioselectivity
Structure-function relationships
Substrates
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Summary:Family 1 UDP‐glycosyltransferases (UGTs) are known to glycosylate multiple secondary plant metabolites and have been extensively studied. The increased availability of plant genome resources allows the identification of wide gene families, both functional and organizational. In this investigation, two MpUGT isoforms were cloned and functionally characterized from liverworts marchantia polymorpha and had high glycosylation activity against several flavonoids. MpUGT735A2 protein, in particular, tolerates a wide spectrum of substrates (flavonols, flavanones, flavones, stilbenes, bibenzyls, dihydrochalcone, phenylpropanoids, xanthones, and isoflavones). Overexpression of MpUGT735A2 and MpUGT743A1 in Arabidopsis thaliana enhances the accumulation of 3‐ O ‐glycosylated flavonol (kaempferol 3‐ O ‐glucoside‐7‐ O ‐rhamnose), consistent with its in vitro enzymatic activity. Docking and mutagenesis techniques were applied to identify the structural and functional properties of MpUGT735A2 with promiscuous substrates. Mutation of Pro87 to Ser, or Gln88 to Val, substantially altered the regioselectivity for luteolin glycosylation, predominantly from the 3′‐ O ‐ to the 7‐ O ‐position. The results were elucidated by focusing on the novel biocatalysts designed for producing therapeutic flavonoids. This investigation provides an approach to modulate MpUGT735A2 as a candidate gene for diverse glycosylation catalysis and a tool to design GTs with new substrate specificities for biomedical applications.
ISSN:0021-9541
1097-4652
DOI:10.1002/jcp.31101