Heterologous expression and characterization of functional mushroom tyrosinase (AbPPO4)
نویسندگان
چکیده
منابع مشابه
Latent and active abPPO4 mushroom tyrosinase cocrystallized with hexatungstotellurate(VI) in a single crystal
Tyrosinases, bifunctional metalloenzymes, catalyze the oxidation of monophenols and o-diphenols to o-quinones, the precursor compounds of the brown-coloured pigment melanin. In eukaryotic organisms, tyrosinases are expressed as latent zymogens that have to be proteolytically cleaved in order to form highly active enzymes. This activation mechanism, known as the tyrosinase maturation process, ha...
متن کاملPurification and Characterization of Melanogenic Enzyme Tyrosinase from Button Mushroom
Melanogenesis is a biosynthetic pathway for the formation of the pigment melanin in human skin. A key enzyme, tyrosinase, catalyzes the first and only rate-limiting steps in melanogenesis. Since the discovery of its melanogenic properties, tyrosinase has been in prime focus and microbial sources of the enzyme are sought. Agaricus bisporus widely known as the common edible mushroom, it's taking ...
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Background: Subunit vaccines are appropriate vaccine candidates for the prevention of some infections. In this study, three immunogenic proteins of Mycobacterium tuberculosis, including HspX, Ppe44, and EsxV as a new construction, were expressed alone and as a fusion protein to develop a new vaccine candidate against tuberculosis infection. Methods: To make the fusion protein, the three genes ...
متن کاملPhysicochemical and kinetic properties of mushroom tyrosinase.
Tyrosinase (o-diphenol: O2 oxidoreductase, EC 1.10.3.1) has been purified from a commercial lyophilized powder prepared from edible mushrooms. Specific activities toward DL-dihydroxyphenylalanine and catechol, homogeneity, molecular weight, absorption spectrum, amino acid composition, and copper content of the preparation are comparable to other purified samples of tyrosinase prepared from fres...
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ژورنال
عنوان ژورنال: Scientific Reports
سال: 2017
ISSN: 2045-2322
DOI: 10.1038/s41598-017-01813-1