Article citationsMore>>

Turner, J.J., Gerrard, J.A. and Hutton, C.A. (2005) Heterocyclic inhibitors of dihydrodipicolinate synthase are not competitive. Bioorganic & Medicinal Chemistry, 13, 2133-2140. doi:10.1016/j.bmc.2005.01.001

has been cited by the following article:

• TITLE: Insilico studies of 2-methylheptyl isonicotinate produced by Streptomyces sps. 201 against dihydrodipicolinate synthase enzyme of Mycobacterium tuberculosis

  AUTHORS: Salam Pradeep Singh, Rajib Lochan Bezbaruah, Tarun Chandra Bora

  KEYWORDS: DHDPS; Molecular Docking; Hydrogen Bonding

  JOURNAL NAME: Journal of Biophysical Chemistry, Vol.3 No.3, August 28, 2012

  ABSTRACT: Tuberculosis is thought to have infected one-third of the world’s population and antibiotic resistance is a growing problem in multi-drug-resistant tuberculosis which is caused by Mycobacterium tuberculosis (MTB). It has been reported that Mycobacterial cell walls are characterized by high DAP (diaminopimelic acid) content—an intermediate of the (S)-lysine biosynthetic pathway. Hence, the Lysine/DAP biosynthetic pathway is a promising target because of its role in cell wall and amino acid biosynthesis. In this study we performed a molecular docking analysis of a novel antibacterial isolated from Streptomyces sps. 201 against dihydrodipicolinate synthase (DHDPS) enzyme of Mycobacterium tuberculosis. The docking studies suggest that the novel molecule binds at active site LYS 171 forming a cleft and at other potential ligand binding site exhibiting all the major interactions such as hydrogen bonding, hydrophobic interaction and electrostatic interaction with (THR55, TYR143, ARG148, LYS171, VAL257 and GLY256) residues.