Specificity analysis and mechanism of aurone synthesis catalyzed by aureusidin synthase, a polyphenol oxidase homolog responsible for flower coloration

被引:92
作者
Nakayama, T
Sato, T
Fukui, Y
Yonekura-Sakakibara, K
Hayashi, H
Tanaka, Y
Kusumi, T
Nishino, T
机构
[1] Tohoku Univ, Grad Sch Engn, Dept Biomol Engn, Sendai, Miyagi 9808579, Japan
[2] Suntory Ltd, Inst Fundamental Res, Shimamoto, Osaka 6188503, Japan
[3] Osaka Med Coll, Dept Biochem, Takatsuki, Osaka 5698686, Japan
关键词
aurone; aureusidin synthase; bracteatin; 2 ',4,4 ',6 '-tetrahydroxychalcone; 2 ',3,4,4 ',6 '-pentahydroxychalcone; polyphenol oxidase; tyrosinase;
D O I
10.1016/S0014-5793(01)02529-7
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Aureusidin synthase, which plays a key role in the yellow coloration of snapdragon flowers, is a homolog of plant polyphenol oxidase (PPO), The enzyme specifically acted on chalcones with a il-monohydroxy or 3,4-dihydroxy B-ring to produce aurones, for whose production the oxidative cyclization of chalcones must be preceded by 3-osygenation, However, it exhibited virtually no PPO activity toward non-chalcone phenolics. The enzyme was competitively inhibited by phenylthiourea, a specific PPO inhibitor. These results led us to propose a mechanism of aurone synthesis by areusidin synthase on the basis of known PPO-catalyzed reactions and conclude that the enzyme is a chalcone-specific PPO specialized for aurone biosynthesis. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B,V, All rights reserved.
引用
收藏
页码:107 / 111
页数:5
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