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Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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Cloning and characterization of phosphomannose isomerase from sphingomonas chungbukensis DJ77

  • Tran, Sinh Thi (Deparments of Biochemistry, Chungbuk National University) ;
  • Le, Dung Tien (Deparments of Biochemistry, Chungbuk National University) ;
  • Kim, Young-Chang (Deparments of Microbiology, Chungbuk National University) ;
  • Shin, Malshik (Department of Food and Nutrition, Chonnam National University) ;
  • Choi, Jung-Do (Deparments of Biochemistry, Chungbuk National University)
  • Published : 2009.08.31
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Abstract

Phosphomannose isomerase (PMI) catalyzes the interconversion of fructose-6-phosphate and mannose-6-phosphate in the extracellular polysaccharide (EPS) synthesis pathway. The gene encoding PMI in Sphingomonas chungbukensis DJ77 was cloned and expressed in E. coli. The pmi gene is 1,410 nucleotides long and the deduced amino acid sequence shares high homology with other bifunctional proteins that possess both PMI and GDP-mannose pyrophosphorylase (GMP) activities. The sequence analysis of PMI revealed two domains with three conserved motifs: a GMP domain at the N-terminus and a PMI domain at the C-terminus. Enzyme assays using the PMI protein confirmed its bifunctional activity. Both activities required divalent metal ions such as $Co^{2+}$, $Ca^{2+}$, $Mg^{2+}$, $Ni^{2+}$ or $Zn^{2+}$. Of these ions, $Co^{2+}$ was found to be the most effective activator of PMI. GDP-D-mannose was found to inhibit the PMI activity, suggesting feedback regulation of this pathway.

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References

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