Functional identification and characterization of two flavonoid glycosyltransferases ZmUGT84A3 and ZmUGT84A4 from maize
文献类型： 外文期刊
作者： Ke, Zhao 1 ; Zheng, Dengyu 2 ; She, Meng 2 ; Zhang, Shipeng 2 ; Wu, Zhongyi 2 ; Lu, Min 1 ; Zhang, Zhongbao 2 ;
作者机构： 1.Beijing Univ Agr, Coll Plant Sci & Technol, Beijing, Peoples R China
2.Beijing Acad Agr & Forestry Sci, Beijing Key Lab Agr Genet Resources & Biotechnol, Inst Biotechnol, Beijing, Peoples R China
3.Yangtze Univ, Coll Agr, Jingzhou, Hubei, Peoples R China
关键词： Uridine diphosphate glycosyltransferases; Maize; Flavonoid; Luteolin; In vitro experiments
期刊名称：JOURNAL OF PLANT BIOCHEMISTRY AND BIOTECHNOLOGY （ 影响因子：1.9； 五年影响因子：1.6 ）
ISSN： 0971-7811
年卷期： 2024 年 33 卷 2 期
页码：
收录情况： SCI
摘要： Luteolin is an important secondary metabolite of maize, which can be glycosylated through uridine diphosphate glycosyltransferase (UGT). Extensive research on UGT has been centered in Arabidopsis thaliana, but little in maize. We cloned two maize glycosyltransferase genes, ZmUGT84A3 and ZmUGT84A4. In vitro experiments revealed that ZmUGT84A3 and ZmUGT84A4 glycosylated luteolin to both luteolin-7-O-glucoside and luteolin-4 ',7-di-O-glucoside. Notably, both ZmUGT84A3 and ZmUGT84A4 catalyzed glycosylation of many flavonoids including apigenin, naringenin, eriodyctiol, kaempferol, and quercetin. Increased temperature enhanced activities of both ZmUGT84A3 and ZmUGT84A4, and elevated a production of luteolin-4 ',7-di-O-glucoside. ZmUGT84A3 activity was optimal under acidic conditions but ZmUGT84A4 preferred alkaline environments. ZmUGT84A4 exhibited higher catalytic activities (1.3 to 2.6-fold) at various substrate concentrations than did ZmUGT84A3; the latter enzyme evidenced a unique activity pattern. Enzyme-catalyzed reaction processes of ZmUGT84A3 and ZmUGT84A4 in vitro for luteolin were depicted. This study unveiled two novel multifunctional glycosyltransferases identified in maize, which exhibited extensive substrate specificity, possessed multiple catalytic sites, and offered valuable insights for studying their enzymatic characteristics.
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