In Vitro Enzymatic Conversion of Glibenclamide Using Squalene Hopene Cyclase from Pseudomonas mendocina Expressed in E. coli BL21 (DE3)
Autor: | Kochupurackal Jayachandran, Indu M Nair |
---|---|
Rok vydání: | 2020 |
Předmět: |
0106 biological sciences
Pseudomonas mendocina Bioengineering Squalene-hopene cyclase 01 natural sciences Applied Microbiology and Biotechnology Biochemistry Glibenclamide 03 medical and health sciences Squalene chemistry.chemical_compound Biotransformation Bacterial Proteins 010608 biotechnology Glyburide medicine Escherichia coli Molecular Biology Intramolecular Transferases 030304 developmental biology chemistry.chemical_classification 0303 health sciences biology biology.organism_classification In vitro Recombinant Proteins Enzyme chemistry Docking (molecular) Biotechnology medicine.drug |
Zdroj: | Molecular biotechnology. 62(9) |
ISSN: | 1559-0305 |
Popis: | Squalene hopene cyclases catalyse the conversion of a linear substrate squalene to a cyclic product with high stereo-selectivity.The enzyme squalene hopene cyclase from Pseudomonas mendocina expressed in E. coli BL21 (DE3) was evaluated for its synthetic drug transforming ability. Nine synthetic drugs were selected as substrates for biotransformation reactions by the enzyme. The homology modelling of the protein and docking of the selected ligands were performed using GOLD suite docking software. The drug which showed maximum binding with the active-site residues of the enzyme was selected for biotransformation studies. On transformation with the enzyme, Glibenclamide, the selected antidiabetic drug alone showed significant changes in the FT/IR spectra; hence, it was selected for LCMS analysis to confirm the transformations. From the chromatogram and MS spectra, the mono-oxygenation of the product due to the enzymatic activity was confirmed. The drug transforming ability of the purified SHC could be used as an ideal tool for the generation of new and active substrate derivatives. |
Databáze: | OpenAIRE |
Externí odkaz: |