In vitro experimental study demonstrates enhanced catecholase activity in recombinant human tyrosinase, suggesting useful industrial and medical applications.
BACKGROUND: Tyrosinases are copper-containing enzymes that initiate the melanin synthesis. They catalyze the direct oxidation of L-tyrosine or L-DOPA into L-DOPAquinone. OBJECTIVES: In present study, we aimed to obtain a recombinant tyrosinase with enhanced catecholase activity through site-directed mutagenesis. MATERIALS AND METHODS: ions tripled catecholase activity of the recombinant protein. Therefore, all mutants were obtained under similar conditions. RESULTS: hydrogen bond occurs between side chain carboxyl oxygens of D374 and H367 in M374D. In the wild-type tyrosinase, the peptide oxygen atom of M374 is responsible for hydrogen bonding with H367. CONCLUSIONS: Our data suggests that M374D mutational variant has applications in different areas such as agriculture, industry, and medicine.
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Shahrisa et al. (2020) studied this question.
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