ArticleIranian journal of biotechnology2020
Enhancing Catecholase Activity of a Recombinant Human Tyrosinase Through Multiple Strategies.
Article in Iranian journal of biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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1 citing paper in PubMed, 2 citations in OpenAlex.
- Interaction Between Florfenicol and Doxycycline Involving Cytochrome P450 3A in Goats (Frontiers in veterinary science · 2021Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundTyrosinases are copper-containing enzymes that initiate the melanin synthesis. They catalyze the direct oxidation of L-tyrosine or L-DOPA into L-DOPAquinone.
objectivesIn present study, we aimed to obtain a recombinant tyrosinase with enhanced catecholase activity through site-directed mutagenesis. MATERIALS AND
methodsThe coding sequence of human tyrosinase along with native signal sequence was cloned into pET-28a (+). BL-21 was used as expression host and recombinant protein was purified by Ni-NTA resins. Site-directed mutagenesis was performed on M374 residue to achieve four mutants: M374D, M374T, M374K and M374R. Chloride ions (Cl
resultsAlthough all the mutants presented higher catecholase activity in comparison to the wild-type enzyme, a significant increase in catecholase activity of the M374D mutant was observed ‒ 13.2-fold.
conclusionsOur data suggests that M374D mutational variant has applications in different areas such as agriculture, industry, and medicine.
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