Chie Suzuki-Ogoh

National Institute of Advanced Industrial Science and Technology, Ōsaka-shi, Osaka-fu, Japan

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Publications (2)5.25 Total impact

  • Article: C-terminal region of the active domain enhances enzymatic activity in dinoflagellate luciferase.
    Chie Suzuki-Ogoh, Chun Wu, Yoshihiro Ohmiya
    [show abstract] [hide abstract]
    ABSTRACT: The dinoflagellate luciferase of Lingulodinium polyedrum has three catalytic domains in its single polypeptide chain (M(r) = 137 kDa), and each 42 kDa domain is enzymatically active. Deletion mutants for N- or C-terminal regions of domain 3 of the luciferase, ranging from 29 to 38 kDa, were constructed and expressed in E. coli cells. The activities of N-terminal deleted mutants were above 20% of wild type, but showed different pH-activity profiles. By contrast, the activities of C-terminal deleted mutants decreased drastically to below 1% of wild type, although their pH-activity profiles and spectra were identical to those of wild type L. polyedrum luciferase. These results indicate that the C-terminal region of this enzyme could be important for the bioluminescence reaction, although based on crystal structure of the luciferase domain, this region does not contain active or regulatory sites.
    Photochemical and Photobiological Sciences 03/2008; 7(2):208-11. · 2.58 Impact Factor
  • Article: Dual-reporter assay using two secreted luciferase genes.
    Chun Wu, Chie Suzuki-Ogoh, Yoshihiro Ohmiya
    BioTechniques 03/2007; 42(3):290, 292. · 2.67 Impact Factor

Institutions

  • 2008
    • National Institute of Advanced Industrial Science and Technology
      • Research Center for Stem Cell Engineering
      Ōsaka-shi, Osaka-fu, Japan