Exploration of the Substrate Diversity of Leucoanthocyanidin Reductases
Exploration of the Substrate Diversity of Leucoanthocyanidin Reductases
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无色花青素还原酶底物多样性的探索
DOI:
10.1021/acs.jafc.9b06353
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发表时间:
2020
影响因子:
6.1
通讯作者:
Xia Tao
中科院分区:
文献类型:
--
作者:
Zhang Lingjie;Wang Peiqiang;Ma Xue;Zhao Wenyan;Li Ming;Yao Shengbo;Liu Yajun;Gao Liping;Xia Tao
Proanthocyanidins (PAs) are mainly composed of epicatechin (EC) or catechin (C) subunits. C-type catechins (C and GC) are generally considered to be catalyzed by leucocyanidin reductase (LAR). In this study, we re-evaluated the function of LAR.LcLAR1was isolated fromLotus corniculatus, which is rich in C-type catechins. Overexpression ofLcLAR1in tobacco resulted in a significantly increased content of EC and EC-glucoside. Overexpression ofLcLAR1inArabidopsis thalianapromoted the accumulation of soluble PAs, including EC, PA dimers, and PA trimers. However, in the transgenicansmutant overexpressingLcLAR1, the contents of C and C-glucoside were increased. In addition, overexpression ofLcLAR1inL. corniculatusresulted in a significant increase of C levels. Taken together, the products ofLcLAR1 depended on the substrates, which revealed the substrate diversity ofLcLAR1. Our study provides new insights into the flavonoid pathway, especially the role of LAR.