title: Computational modelling and protein-ligand interaction studies of SMlipA lipase cloned from forest metagenome.
abstract: The understanding of the 3-dimensional enzyme structure is important for the point of protein engineering and applications. Computer-based molecular modelling is a vital tool for theoretical predication of enzyme activities and finding their substrates and inhibitors. SMlipA lipase was cloned from forest soil metagenome and characterized as broad spectrum enzyme with high stability in various organic solvents. In the present study, to understand the mechanism of SMlipA lipase and to identify the key residues involved in enzyme-substrate interaction, three dimensional-computational model of SMlipA has been generated and validated for stereo-chemical and amino-acid environment quality using appropriate programs, and further validation of the active-site architecture was achieved by performing docking studies with different ligand. The three dimensional structure created here provide a new understanding of the ligand preferences and their interaction with protein.
authors: CSIR-Central Food Technological Research Institute, Resource Centre Lucknow, 226018 India. Electronic address: mahejibin@cftri.org.
authors: Mahejibin
authors: M
authors: Khan
authors: Public Health Foundation of India, Plot 47, Sector 44, Gurgaon 122002 National Capital Region, India.
authors: Amit
authors: A
authors: Kumar
mesh_terms: D000595:Amino Acid Sequence; D020134:Catalytic Domain; D065928:Forests; D020407:Internet; D008024:Ligands; D008049:Lipase / Q000737:chemistry*; D054892:Metagenome; D008958:Models, Molecular; D017433:Protein Structure, Secondary; D015203:Reproducibility of Results; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
chemical_list: D008024:Ligands; D008049:Lipase
keywords: Metagenomics; Molecular modeling; Protein interaction; Solvent stable lipase