Insilico studies of 2-methylheptyl isonicotinate produced by Streptomyces sps. 201 against dihydrodipicolinate synthase enzyme of Mycobacterium tuberculosis
作者: Salam Pradeep SinghRajib Lochan BezbaruahTarun Chandra Bora
作者单位: 1Bioinformatics Infrastructure Facility, Biotechnology Division, North-East Institute of Science & Technology, Jorhat, India
刊名: Journal of Biophysical Chemistry, 2012, Vol.3 (3), pp.233-237
来源数据库: Scientific Research Publishing Journal
DOI: 10.4236/jbpc.2012.33027
关键词: DHDPSMolecular DockingHydrogen Bonding
原始语种摘要: 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...
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关键词翻译
关键词翻译
  • Mycobacterium -ria
  • tuberculosis 肺结核
  • against 反对
  • synthase 合酶
  • enzyme 
  • pathway 轨道
  • biosynthetic 生物合成
  • docking 靠泊
  • antibiotic 抗生素
  • resistant 耐久的