User talk:Himtifr

Effect of various metal ions on activity of lipases and its use in resolution of chiral drugs
Many drugs, pharmaceuticals and flavor compounds are chiral molecules with each enantiomer having different biological activity. In some cases, only one of the enantiomers has the desired activity, while the other enantiomer may produce undesirable side effects. Thus, the production of chiral products in single- enantiomer form is an important task. In this study, the task can be achieved by using Lipase from microbial source which can be isolated from a nearby pond, oil mills and soil for the resolution of racemic drugs and the separation was accomplished by means of the formation of single enantiomer. Three-dimensional structures of bacterial lipases were solved to understand the catalytic mechanism of lipase reactions. Structural characteristics include a hydrolase fold, a catalytic triad consisting of a nucleophilic serine located in a highly conserved Gly-X-Ser-X-Gly pentapeptide, and an aspartate or glutamate residue that is hydrogen bonded to a histidine. Four substrate binding pockets has been identified for triglycerides: an oxyanion hole and three pockets accommodating the fatty acids bound at positions sn-1, sn-2, and sn-3. The differences in size and the hydrophilicity/hydrophobicity of these pockets determine the enantiopreference of a lipase. The understanding of structure-function relationships will enable researchers to tailor new lipases for biotechnological applications. At the same time, directed evolution in combination with appropriate effect with various metal ions (i.e. Ca2+, Mg2+, Mn2+, Na+, K+, Cu2+) can also be studied to assay lipase activity to get better resolution of chiral drugs.

Keywords: 	enantiomer, chiral, resolution, racemic drugs, metal ions