Cloning, Expression, and Functional Characterization of Two Highly Efficient Flavonoid-di- O -glycosyltransferases ZmUGT84A1 and ZmUGT84A2 from Maize ( Zea mays L.).
Xiaorong SunZhao KeDengyu ZhengMeng SheZhongyi WuQing X LiZhong-Bao ZhangPublished in: Journal of agricultural and food chemistry (2024)
The maize ( Zea mays L.) glycosyltransferase family 1 comprises many uridine diphosphate glycosyltransferase (UGT) members. However, UGT activities and biochemical functions have seldom been revealed. In this study, the genes of two flavonoid di- O -glycosyltransferases ZmUGT84A1 and ZmUGT84A2 were cloned from maize plant and expressed in Escherichia coli . Phylogenetic analysis showed that the two enzymes were homologous to AtUGT84A1 and AtUGT84A3. The two recombinant enzymes showed a high conversion rate of luteolin to its glucosides, mainly 4',7-di- O -glucoside and minorly 3',7-di- O -glucoside in two-step glycosylation reactions in vitro . Moreover, the recombinant ZmUGT84A1 and ZmUGT84A2 had a broad substrate spectrum, converting eriodictyol, naringenin, apigenin, quercetin, and kaempferol to monoglucosides and diglucosides. The highly efficient ZmUGT84A1 and ZmUGT84A2 may be used as a tool for the effective synthesis of various flavonoid O -glycosides and as markers for crop breeding to increase O -glycosyl flavonoid content in food.
Keyphrases
- highly efficient
- biofilm formation
- escherichia coli
- poor prognosis
- pseudomonas aeruginosa
- staphylococcus aureus
- climate change
- dna damage
- candida albicans
- cell free
- gene expression
- oxidative stress
- long non coding rna
- cystic fibrosis
- dna methylation
- transcription factor
- human health
- genome wide identification
- genome wide analysis