The in vitro characterization of the iterative avermectin glycosyltransferase AveBI reveals reaction reversibility and sugar nucleotide flexibility
The in vitro characterization of the iterative avermectin glycosyltransferase AveBI reveals reaction reversibility and sugar nucleotide flexibility
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DOI：
10.1021/ja065950k
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发表时间：
2006-12-27
影响因子：
15
通讯作者：
Thorson, Jon S.
中科院分区：
文献类型：
--
作者：
Zhang, Changsheng;Albermann, Christoph;Thorson, Jon S.
对参与大环内酯类抗虫阿维菌素（AVM）生物合成的糖基转移酶AveBI进行了体外表征。AveBI催化了两次独立的夹竹桃的迭代加成，并证明了AveBI催化反应的可逆性。对糖核苷酸特异性的研究揭示了10种独特的糖核苷酸底物，它们与5种不同的苷元结合，导致产生50种不同糖基化的AVM变体。
The glycosyltransferase AveBI, which is involved in the biosynthesis of the macrolide antihelmintic avermectin (AVM), was characterized in vitro. AveBI was confirmed to catalyze two separate iterative additions ofl-oleandrose, and the reversibility of AveBI-catalyzed reaction was also demonstrated. Investigation of sugar nucleotide specificity revealed 10 unique sugar nucleotide substrates which, in combination with five distinct aglycones, led to the production of 50 differentially glycosylated AVM variants.