| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 9616693 | Journal of Molecular Catalysis B: Enzymatic | 2005 | 8 Pages |
Abstract
GDP-mannose pyrophosphorylase gene (ManC) of Escherichia coli (E. coli) O157 was cloned and expressed as a highly soluble protein in E. coli BL21 (DE3). The enzyme was subsequently purified using hydrophobic and ion exchange chromatographies. ManC showed very broad substrate specificities for four nucleotides and various hexose-1-phosphates, yielding ADP-mannose, CDP-mannose, UDP-mannose, GDP-mannose, GDP-glucose and GDP-2-deoxy-glucose.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Catalysis
Authors
Yung-Hun Yang, Young-Bok Kang, Kwang-Won Lee, Tek-Hyung Lee, Sung-Soo Park, Bum-Yeol Hwang, Byung-Gee Kim,