Computational study of the hydroxylation and epoxidation by the mutants of the PaDa-I peroxygenase variant

Identifier:  TFG:4452

Handle: https://hdl.handle.net/20.500.11797/TFG4452

Authors:  Martínez Sugrañes, Mireia

Abstract:
Unspecific peroxygenases (UPOs) represent a new family of fungal heme-thiolate enzymes with high biotechnological interest. Many of these enzymes have been engineered, combining rational and directed evolution tools with computational design methods, to obtain the required selectivity, efficiency, and stability. For this purpose, the Protein Energy Landscape Exploration (PELE) software has been used. Using as departure point the UPO mutant from Agrocybe aegerita PaDa-I, we characterized the specificity, regio- and enantioselectivity of thirty mutants against five substrates. In the future, these results will help to perform both retrospective and prospective analysis to combine the best mutations in new variants.