TY - JFULL AU - Jayashree Ramana PY - 2013/8/ TI - Novel Structural Insights of Glutamate Racemase from Mycobacterium tuberculosis through Modeling and Docking Studies T2 - International Journal of Medical and Health Sciences SP - 417 EP - 422 VL - 7 SN - 1307-6892 UR - https://publications.waset.org/pdf/16514 PU - World Academy of Science, Engineering and Technology NX - Open Science Index 79, 2013 N2 - An alarming emergence of multidrug-resistant strains of the tuberculosis pathogen Mycobacterium tuberculosis and continuing high worldwide incidence of tuberculosis has invigorated the search for novel drug targets. The enzyme glutamate racemase (MurI) in bacteria catalyzes the stereoconversion of L-glutamate to D-glutamate which is a component of the peptidoglycan cell wall of the bacterium. The inhibitors targeted against MurI from several bacterial species have been patented and are advocated as promising antibacterial agents. However there are none available against MurI from Mycobacterium tuberculosis, due to the lack of its threedimensional structure. This work accomplished two major objectives. First, the tertiary structure of MtMurI was deduced computationally through homology modeling using the templates from bacterial homologues. It is speculated that like in other Gram-positive bacteria, MtMurI exists as a dimer and many of the protein interactions at the dimer interface are also conserved. Second, potent candidate inhibitors against MtMurI were identified through docking against already known inhibitors in other organisms. ER -