Characterization of GDP-mannose Pyrophosphorylase from Escherichia Coli O157:H7 EDL933 and Its Broad Substrate Specificity

Authors

Yung-Hun Yang, Seoul National University
Young Bok (Abraham) Kang, George Fox UniversityFollow
Kwang-Won Lee, Seoul National University
Tek-Hyung Lee, Seoul National University
Sung-Soo Park, Seoul National University
Bum-Yeol Hwang, The University of Texas-Austin
Byung-Gee Kim, Seoul National University

Document Type

Article

Publication Date

12-2005

Publication Title

Journal of Molecular Catalysis B: Enzymatic

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.

Keywords

GDP-mannose pyrophosphorylase; NDP-mannose; ESI-MS; Substrate specificity

Volume

37

Issue

1-6

First Page

1

Last Page

8

DOI

https://doi.org/10.1016/j.molcatb.2005.08.002

ISSN

1381-1177

Comments

Originally published in Journal of Molecular Catalysis B: Enzymatic 37 (2005) 1–8, Elsevier.

https://doi.org/10.1016/j.molcatb.2005.08.002

Recommended Citation

Yang, Yung-Hun; Kang, Young Bok (Abraham); Lee, Kwang-Won; Lee, Tek-Hyung; Park, Sung-Soo; Hwang, Bum-Yeol; and Kim, Byung-Gee, "Characterization of GDP-mannose Pyrophosphorylase from Escherichia Coli O157:H7 EDL933 and Its Broad Substrate Specificity" (2005). Faculty Publications - Biomedical, Mechanical, and Civil Engineering. 63.
https://digitalcommons.georgefox.edu/mece_fac/63