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Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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Alteration of The Quaternary Structure of Human UDP-Glucose Dehydrogenase by a Double Mutation

  • Huh, Jae-Wan (Department of Biochemistry and Molecular Biology, University of Ulsan College of Medicine) ;
  • Yang, Seung-Ju (Department of Biomedical Laboratory Science, Konyang University) ;
  • Hwang, Eun-Young (Department of Biochemistry and Molecular Biology, University of Ulsan College of Medicine) ;
  • Choi, Myung-Min (Department of Biochemistry and Molecular Biology, University of Ulsan College of Medicine) ;
  • Lee, Hyun-Ju (Department of Biochemistry and Molecular Biology, University of Ulsan College of Medicine) ;
  • Kim, Eun-A (Department of Biochemistry and Molecular Biology, University of Ulsan College of Medicine) ;
  • Choi, Soo-Young (Department of Biomedical Sciences, Hallym University) ;
  • Choi, Jene (Department of Pathology, University of Ulsan College of Medicine) ;
  • Hong, Hea-Nam (Department of Anatomy and Cell Biology, University of Ulsan College of Medicine) ;
  • Cho, Sung-Woo (Department of Biochemistry and Molecular Biology, University of Ulsan College of Medicine)
  • Published : 2007.09.30
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Abstract

There are conflicting views for the polymerization process of human UDP-glucose dehydrogenase (UGDH) and no clear evidence has been reported yet. Based on crystal coordinates for Streptococcus pyogenes UGDH, we made double mutant A222Q/S233G. The double mutagenesis had no effects on expression, stability, and secondary structure. Interestingly, A222Q/S233G was a dimeric form and showed an UGDH activity, although it showed increased $K_m$ values for substrates. These results suggest that Ala222 and Ser233 play an important role in maintaining the hexameric structure and the reduced binding affinities for substrates are attributable to its altered subunit communication although quaternary structure may not be critical for catalysis.

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References

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