Shin Ichi Ozaki

Summary

Affiliation: Yamaguchi University
Country: Japan

Publications

  1. ncbi request reprint Modulation of cystathionine beta-synthase activity by the Arg-51 and Arg-224 mutations
    Shin Ichi Ozaki
    Department of Biological Sciences, Yamaguchi University, Yamaguchi, Japan
    Biosci Biotechnol Biochem 72:2318-23. 2008
  2. ncbi request reprint Mutagenesis studies of human cystathionine beta-synthase: residues important for heme binding and substrate interactions
    Shin Ichi Ozaki
    Department of Biological Sciences, Yamaguchi University, 1677 1 Yoshida, Yamaguchi, 753 8515, Japan
    Protein Pept Lett 17:351-5. 2010

Detail Information

Publications2

  1. ncbi request reprint Modulation of cystathionine beta-synthase activity by the Arg-51 and Arg-224 mutations
    Shin Ichi Ozaki
    Department of Biological Sciences, Yamaguchi University, Yamaguchi, Japan
    Biosci Biotechnol Biochem 72:2318-23. 2008
    ..The results indicate that structural changes in the heme vicinity are transmitted to PLP existing 20 A away from heme. A possible explanation of our results is discussed on the basis of CBS structure...
  2. ncbi request reprint Mutagenesis studies of human cystathionine beta-synthase: residues important for heme binding and substrate interactions
    Shin Ichi Ozaki
    Department of Biological Sciences, Yamaguchi University, 1677 1 Yoshida, Yamaguchi, 753 8515, Japan
    Protein Pept Lett 17:351-5. 2010
    ..Our mutagenesis studies suggest that Arg-266 is important to sense structural changes in heme-binding site, and that Gln-222 as well as Tyr-223 are involved in interactions with substrates...