文档介绍：Synthesis of GDP-mannose in binant
Escherichia coli
Yu Li, Dong-jun Kong, Fu-ping Lu *, Tao Niu, Hong-hong Jia, Ke He
Key Laboratory of Industrial Microbiology, Ministry of Education,
College of Biotechnology, Tianjin University of Science and Technology
Tianjin 300457, P. R. China
29191687@, ******@tust.
Abstract — Three binant Escherichia coli strains processes, for example, prevention of pathogen infection,
were constructed to produce guanosine 5’-diphosphate improvement of immune system response, reduction of
(GDP)-mannose, donor of GDP-fucose, which is an inflammatory processes, and many other events [4]. Since
essential substrate for synthesis of harides. fucosylated harides such as mono- and
Glucokinase (glk), phosphomannomutase (manB), and difucosyllactose and their fucosylated derivatives are
mannose-1-phosphate guanylytransferase (manC), are similar to the glycoproteins and glycolipids of the epithelial
three crucial enzymes for the de novo GDP-mannose cell surface, specific interactions of harides
biosynthesis, were overexpressed in binant by with pathogenic anisms prevent the attachment of
constructing inducible overexpression vectors. The the microbes to epithelial cells [5, 6].
optimum expression conditions for GLK, ManB, and Variation in the activities of the 2- and 3/4-
ManC in binant BL21 (DE3) were 25 ºC