Molecular docking and in silico studies on analogues of 2-methylheptyl isonicotinate with DHDPS enzyme of Mycobacterium tuberculosis
作者: Salam Pradeep SinghBolin Kumar KonwarRajib Lochan BezbaruahTarun Chandra Bora
作者单位: 1Bioinformatics Infrastructure Facility, Department of Molecular Biology and Biotechnology, Tezpur University
2Bioinformatics Infrastructure Facility, Biotechnology Division, North-East Institute of Science and Technology
刊名: Medicinal Chemistry Research, 2013, Vol.22 (10), pp.4755-4765
来源数据库: Springer Nature Journal
DOI: 10.1007/s00044-013-0488-5
关键词: DHDPS enzymeMolecular docking2-Methylheptyl isonicotinateADME-toxicity
原始语种摘要: Abstract(#br) Mycobacterium tuberculosis and other strains of mycobacteria cause tuberculosis which has infected one-third of the world’s population. Moreover, there has been increase in multidrug-resistant strains which spotlights the need for a new anti-tuberculosis drug. The cell wall of mycobacteria is characterised by high diaminopimelic acid (DAP) content—an intermediate of the ( S )-lysine biosynthetic pathway and dihydrodipicolinate synthase (DHDPS) enzyme catalyses the first unique reaction of this biosynthesis. Interestingly, the gene knockout experiment demonstrates the essentiality of the DAP pathway, where the absence of DAP results in cell lysis and death. Because of this importance, any inhibitor of DHDPS enzyme may indicate a new class of anti-tubercular agent. In this...
全文获取路径: Springer Nature  (合作)
影响因子:1.612 (2012)

  • Mycobacterium -ria
  • tuberculosis 肺结核
  • docking 靠泊
  • enzyme