<i>Insilico</i>studies of 2-methylheptyl isonicotinate produced by <i>Streptomyces</i>sps. 201 against dihydrodipicolinate synthase enzyme of <i>Mycobacterium tuberculosis</i>  

作　　者：Salam Pradeep Singh Rajib Lochan Bezbaruah Tarun Chandra Bora 

机构地区：[1]Bioinformatics Infrastructure Facility, Biotechnology Division, North-East Institute of Science & Technology, Jorhat, India

出　　处：《Journal of Biophysical Chemistry》2012年第3期233-237,共5页生物物理化学（英文）

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 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.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.

关 键 词：DHDPS Molecular Docking Hydrogen Bonding 

分 类 号：O6[理学—化学]