• DocumentCode
    3310554
  • Title

    Structural Similarities Between the Catalytic Domain of Threonine Deaminase and the Mammalian Serine Racemases

  • Author

    Srikeerthana, Kuchi ; De Causmaecker, Patrick

  • Author_Institution
    Dept. of Comput. Sci., Katholieke Univ. Leuven, Kortrijk, Belgium
  • fYear
    2010
  • fDate
    20-21 June 2010
  • Firstpage
    371
  • Lastpage
    373
  • Abstract
    Comparison of a newly found enzyme with its structural homologues results in the prediction of probable regulatory binding sites. Since serine racemases are found to be promising targets for the treatment of disorders related to NMDAR dysfunction, the identification of the structural similarities between serine racemases and their structural homologues might provide structural insights for rational drug design. In this study, we aim to determine the structural similarities between the mammalian serine racemases and the bacterial biosynthetic threonine deaminase.
  • Keywords
    enzymes; microorganisms; molecular biophysics; molecular configurations; NMDAR dysfunction; bacterial biosynthetic threonine deaminase; catalytic domain; drug design; enzyme; mammalian serine racemases; regulatory binding sites; structural homologues; structural similarities; Amino acids; Biochemistry; Communications technology; Computer science; Computer science education; Educational technology; Humans; Proteins; Strontium; X-ray diffraction; Serine racemases; domain; homology; threonine deaminase;
  • fLanguage
    English
  • Publisher
    ieee
  • Conference_Titel
    Advances in Computer Engineering (ACE), 2010 International Conference on
  • Conference_Location
    Bangalore
  • Print_ISBN
    978-1-4244-7154-6
  • Type

    conf

  • DOI
    10.1109/ACE.2010.44
  • Filename
    5532897