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
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;
Conference_Titel :
Advances in Computer Engineering (ACE), 2010 International Conference on
Conference_Location :
Bangalore
Print_ISBN :
978-1-4244-7154-6
DOI :
10.1109/ACE.2010.44