标题:The Function and Catalysis of 2-Oxoglutarate-Dependent Oxygenases Involved in Plant Flavonoid Biosynthesis
作者:Cheng, Ai-Xia; Han, Xiao-Juan; Wu, Yi-Feng; Lou, Hong-Xiang
作者机构:[Cheng, Ai-Xia; Han, Xiao-Juan; Wu, Yi-Feng; Lou, Hong-Xiang] Shandong Univ, Key Lab Chem Biol Nat Prod, Minist Educ, Sch Pharmaceut Sci, Jinan 250012 更多
通讯作者:Lou, HX
通讯作者地址:[Lou, HX]Shandong Univ, Key Lab Chem Biol Nat Prod, Minist Educ, Sch Pharmaceut Sci, 44 West Wenhua Rd, Jinan 250012, Peoples R China.
来源:INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
出版年:2014
卷:15
期:1
页码:1080-1095
DOI:10.3390/ijms15011080
关键词:flavanone 3 beta-hydroxylase; flavone synthase I; flavonoid synthesis;; flavonol synthase; anthocyanidin synthase; 2-ODD oxygenases
摘要:Flavonoids are secondary metabolites derived from phenylalanine and acetate metabolism. They fulfil a variety of functions in plants and have health benefits for humans. During the synthesis of the tricyclic flavonoid natural products in plants, oxidative modifications to the central C ring are catalyzed by four of Fe-II and 2-oxoglutarate dependent (2-ODD) oxygenases, namely flavone synthase I (FNS I), flavonol synthase (FLS), anthocyanidin synthase (ANS) and flavanone 3 beta-hydroxylase (FHT). FNS I, FLS and ANS are involved in desaturation of C2-C3 of flavonoids and FHT in hydroxylation of C3. FNS I, which is restricted to the Apiaceae species and in rice, is predicted to have evolved from FHT by duplication. Due to their sequence similarity and substrate specificity, FLS and ANS, which interact with the alpha surface of the substrate, belong to a group of dioxygenases having a broad substrate specificity, while FNS I and FHT are more selective, and interact with the naringenin beta surface. Here, we summarize recent findings regarding the function of the four 2-ODD oxygenases and the relationship between their catalytic activity, their polypeptide sequence and their tertiary structure.
收录类别:SCOPUS;SCIE
WOS核心被引频次:16
Scopus被引频次:18
资源类型:期刊论文
原文链接:https://www.scopus.com/inward/record.uri?eid=2-s2.0-84892594405&doi=10.3390%2fijms15011080&partnerID=40&md5=543ff8b8ce9a2afc855b7f8b55504c37
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