Abstract
Unspecific peroxygenase (UPO) is a heme-thiolate peroxidase with mono(per)oxygenase activity for the selective oxyfunctionalization of C-H bonds. Fueled by catalytic concentrations of H2O2, which acts as both oxygen donor and as final electron acceptor, this stable, soluble, and extracellular enzyme is a potential biocatalyst for dozens of transformations that are of considerable interest in organic synthesis. In this chapter we describe the main attributes of this versatile enzyme while reflecting on the directed evolution campaigns recently followed in our laboratory that set out to enhance the functional expression of UPO in yeast and improve the activity, as well as approximating its properties to the required industrial standards.
Published Version
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