Mesocarp localization of a bi-functional resveratrol/hydroxycinnamic acid glucosyltransferase of Concord grape (Vitis labrusca)
Mesocarp localization of a bi-functional resveratrol/hydroxycinnamic acid glucosyltransferase of Concord grape (Vitis labrusca)
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DOI：
10.1111/j.1365-313x.2006.02987.x
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发表时间：
2007-02-01
期刊：
影响因子：
7.2
通讯作者：
De Luca, Vincenzo
中科院分区：
文献类型：
--
作者：
Hall, Dawn;De Luca, Vincenzo
白藜芦醇是一种芪类化合物，对人体有良好的保健作用，在包括葡萄（葡萄属）在内的几种植物中作为植物抗毒素组成性产生或积累。葡萄浆果在外果皮中积累芪类化合物，作为白藜芦醇的顺式和反式异构体，以及它们各自的3-O-单葡萄糖苷。从Concord（葡萄属labrusca）葡萄浆果中纯化葡糖基化顺式和反式白藜芦醇的酶至表观同质性，并且肽测序将其与未表征的葡萄属葡萄属全长克隆（TC 38971，TIGR数据库）相关联。来自葡萄属labrusca（VLRSgt）的相应基因与克隆TC 38971具有98%的序列同一性，并且与产生葡萄糖酯的葡萄属葡萄糖苷-羟基苯甲酸葡糖基转移酶具有92%的序列同一性。该重组酶在较宽的pH范围内（5.5-10）是活跃的，产生葡萄糖苷的芪类化合物，黄酮类化合物和香豆素在较高的pH值和葡萄糖酯的几个羟基苯甲酸和羟基肉桂酸在低pH值。葡萄属labrusca葡萄浆果积累的芪葡萄糖苷和羟基肉桂酸葡萄糖酯，符合VLRSgt在芪和羟基肉桂酸修饰的双功能作用。虽然VLRSgt和其他功能特征的葡糖基转移酶的系统发育分析将其与其他葡萄糖酯产生酶，目前的结果表明这类酶的更广泛的生化活性。
Resveratrol is a stilbene with well-known health-promoting effects in humans that is produced constitutively or accumulates as a phytoalexin in several plant species including grape (Vitis sp.). Grape berries accumulate stilbenes in the exocarp as cis- and trans-isomers of resveratrol, together with their respective 3-O-monoglucosides. An enzyme glucosylating cis- and trans-resveratrol was purified to apparent homogeneity from Concord (Vitis labrusca) grape berries, and peptide sequencing associated it to an uncharacterized Vitis vinifera full-length clone (TC38971, TIGR database). A corresponding gene from Vitis labrusca (VLRSgt) had 98% sequence identity to clone TC38971 and 92% sequence identity to a Vitis viniferap-hydroxybenzoic acid glucosyltransferase that produces glucose esters. The recombinant enzyme was active over a broad pH range (5.5-10), producing glucosides of stilbenes, flavonoids and coumarins at higher pH and glucose esters of several hydroxybenzoic and hydroxycinnamic acids at low pH. Vitis labrusca grape berries accumulated both stilbene glucosides and hydroxycinnamic acid glucose esters, consistent with the bi-functional role of VLRSgt in stilbene and hydroxycinnamic acid modification. While phylogenetic analysis of VLRSgt and other functionally characterized glucosyltransferases places it with other glucose ester-producing enzymes, the present results indicate broader biochemical activities for this class of enzymes.