Lellouch A C, Watt G M, Geremia R A, Flitsch S L
CNRS Centre de Recherches sur les Macromolecules Vegetales, associe avec l'Universite Joseph Fourier, Grenoble, France.
Biochem Biophys Res Commun. 2000 May 27;272(1):290-2. doi: 10.1006/bbrc.2000.2771.
The biochemical characterization of bacterial glycosyltransferases involved in the assembly of cell-wall-associated polysaccharides is often hindered by the lack of the appropriate undecaprenyl-pyrophosphate-linked acceptor substrate. In order to find a suitable synthetic substrate for the alpha1,3-mannosyltransferase AceA from Acetobacter xylinum, phytanyl-pyrophosphate-linked cellobiose was prepared. In the presence of GDP-[14C]mannose and recombinant AceA, the phytanyl-pyrophosphate-linked cellobiose afforded a 14C-labeled trisaccharide that was sensitive to alpha-mannosidase degradation in a fashion analogous to the natural undecaprenyl-pyrophosphate-linked cellobiose substrate. These results suggest that phytanyl-pyrophosphate-linked oligosaccharides may be useful substrates for other important bacterial glycosyltransferases.
参与细胞壁相关多糖组装的细菌糖基转移酶的生化特性研究常常因缺乏合适的十一异戊烯焦磷酸连接的受体底物而受阻。为了找到木醋杆菌α1,3-甘露糖基转移酶AceA的合适合成底物，制备了植烷焦磷酸连接的纤维二糖。在GDP-[14C]甘露糖和重组AceA存在的情况下，植烷焦磷酸连接的纤维二糖产生了一种14C标记的三糖，该三糖对α-甘露糖苷酶降解敏感，其方式类似于天然的十一异戊烯焦磷酸连接的纤维二糖底物。这些结果表明，植烷焦磷酸连接的寡糖可能是其他重要细菌糖基转移酶的有用底物。
