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Tyrosinase efficiently catalyzes the  ortho -hydroxylation of monophenols and the oxidation of diphenols without any additional cofactors. Although it is of significant interest for the biosynthesis of catechol derivatives, the rapid catechol oxidase activity and inactivation of tyrosinase have hampered its practical utilization as a monophenol monooxygenase. Here, we prepared a functional tyrosinase that exhibited a distinguished monophenolase/diphenolase activity ratio ( V   max  mono/  V   max  di = 3.83) and enhanced catalytic efficiency against  L -tyrosine ( k    cat   = 3.33 ± 0.18 s −1 ,  K    m   = 2.12 ± 0.14 mM at 20 °C and pH 6.0). This enzyme was still highly active in ice water (>80%), and its activity was well conserved below 30 °C.  In vitro  DOPA modification, with a remarkably high yield as a monophenol monooxygenase, was achieved by the enzyme taking advantage of these biocatalytic properties. These results demonstrate the strong potential for this enzyme’s use as a monophenol monooxygenase in biomedical and industrial applications.

A tyrosinase, mTyr-CNK, that is functionally available as a monophenol monooxygenase