TY - JOUR
T1 - The in vitro characterization of the iterative avermectin glycosyltransferase AveBI reveals reaction reversibility and sugar nucleotide flexibility
AU - Zhang, Changsheng
AU - Albermann, Christoph
AU - Fu, Xun
AU - Thorson, Jon S.
PY - 2006/12/27
Y1 - 2006/12/27
N2 - 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 of l-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.
AB - 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 of l-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.
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U2 - 10.1021/ja065950k
DO - 10.1021/ja065950k
M3 - Article
C2 - 17177349
AN - SCOPUS:33845935524
SN - 0002-7863
VL - 128
SP - 16420
EP - 16421
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
IS - 51
ER -