生物
O-甲基转移酶
系统发育树
甲基化
木脂素
遗传学
甲基转移酶
生物化学
基因
植物
作者
Masaomi Yamamura,Masato Kumatani,Akira Shiraishi,Ming Yu,Keisuke Kobayashi,Atsushi Suzuki,Atsushi Kawamura,Honoo Satake,Safendrri Komara Ragamustari,Shiro Suzuki,Hideyuki Suzuki,Daisuke Shibata,Shinya Kawai,Eiichiro Ono,Toshiaki Umezawa
出处
期刊:Plant and Cell Physiology
[Oxford University Press]
日期:2022-11-22
卷期号:64 (1): 124-147
被引量:3
摘要
O-Methyltransferases (OMTs) play important roles in antitumor lignan biosynthesis. To date, six OMTs catalyzing the methylation of dibenzylbutyrolactone lignans as biosynthetic precursors of antitumor lignans have been identified. However, there is still no systematic understanding of the diversity and regularity of the biosynthetic mechanisms among various plant lineages. Herein, we report the characterization of two OMTs from Anthriscus sylvestris and Thujopsis dolabrata var. hondae [designated as AsSecoNorYatein (SNY) OMT and TdSNYOMT] together with the six known OMTs to evaluate their diversity and regularity. Although A. sylvestris 5-O-methylthujaplicatin (SecoNorYatein) and 4-O-demethylyatein (NorYatein) OMT (AsSNYOMT) and TdSNYOMT accept 5-O-methylthujaplicatin and 4-O-demethylyatein as substrates, phylogenetic analysis indicated that these two OMTs shared low amino acid sequence identity, 33.8%, indicating a signature of parallel evolution. The OMTs and the six previously identified OMTs were found to be diverse in terms of their substrate specificity, regioselectivity and amino acid sequence identity, indicating independent evolution in each plant species. Meanwhile, two-entropy analysis detected four amino acid residues as being specifically acquired by dibenzylbutyrolactone lignan OMTs. Site-directed mutation of AsSNYOMT indicated that two of them contributed specifically to 5-O-methylthujaplicatin methylation. The results provide a new example of parallel evolution and the diversity and regularity of OMTs in plant secondary (specialized) metabolism.
科研通智能强力驱动
Strongly Powered by AbleSci AI