Mudapaka Jagadesh, Taylor Erika Anne
Department of Chemistry, Wesleyan University, Middletown, CT 06459, USA.
Department of Chemistry, Wesleyan University, Middletown, CT 06459, USA.
FEBS Lett. 2015 Jun 4;589(13):1423-9. doi: 10.1016/j.febslet.2015.04.051. Epub 2015 May 7.
Bacterial lipopolysaccharide (LPS) molecules are an important cell surface component that enables adhesion to surfaces and cell motility, amongst other functions. In Escherichia coli, there are multiple Heptosyltransferase enzymes involved in the biosynthesis of the core region of LPS. Here we describe the first ever cloning, expression, purification and characterization of Heptosyltransferase III (HepIII) from E. coli, which catalyzes the addition of an L-glycero-D-manno-heptose (Hep) residue to the growing LPS core via an α(1→7) bond. Inspired by results from our lab on the E. coli HepI, we assessed the catalytic efficiency with phospho-Hep2-Kdo2-Lipid A (PH2K2LA) and two deacylated analogues.
细菌脂多糖（LPS）分子是一种重要的细胞表面成分，除其他功能外，还能实现表面黏附及细胞运动。在大肠杆菌中，有多种庚糖基转移酶参与LPS核心区域的生物合成。在此，我们描述了首次从大肠杆菌中克隆、表达、纯化和鉴定庚糖基转移酶III（HepIII）的过程，该酶通过α(1→7)键催化将一个L-甘油-D-甘露庚糖（Hep）残基添加到正在生长的LPS核心上。受我们实验室关于大肠杆菌HepI的结果启发，我们用磷酸化-Hep2-Kdo2-脂多糖A（PH2K2LA）和两种去酰化类似物评估了催化效率。
