Molecular Interaction of Novel Compound 2-Methylheptyl Isonicotinate Produced by Streptomyces sp. 201 with Dihydrodipicolinate Synthase (DHDPS) Enzyme of Mycobacterium tuberculosis for its Antibacterial Activity
作者: Salam Pradeep SinghT. C. BoraR. L. Bezbaruah
作者单位: 1Bioinformatics Infrastructure Facility, Biotechnology Division, North-East Institute of Science & Technology (CSIR)
刊名: Indian Journal of Microbiology, 2012, Vol.52 (3), pp.427-432
来源数据库: Springer Nature Journal
DOI: 10.1007/s12088-012-0252-4
关键词: DHDPSMolecular dockingAntibiotic resistance
英文摘要: Abstract(#br)Antibiotic resistance is a growing problem in multi-drug-resistant tuberculosis which is caused by Mycobacterium tuberculosis (MTB) . Hence there is an urgent need for designing or developing a novel or potent anti-tubercular agent. The Lysine/DAP biosynthetic pathway is a promising target because of its role in cell wall and amino acid biosynthesis. In our study we performed a molecular docking analysis of a novel antibacterial isolated from Streptomyces sp. 201 at three different binding site of dihydrodipicolinate synthase (DHDPS) enzyme of MTB. The molecular docking studies suggest that the novel molecule shows favourable interaction at the three different binding sites as compared to five experimentally known inhibitors of DHDPS.
全文获取路径: Springer Nature  (合作)
影响因子:0.457 (2012)

  • Mycobacterium -ria
  • tuberculosis 肺结核