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Bioorganic and Medicinal Chemistry, 2014 Tyrosinase is an enzyme widely distributed in the biosphere. It is one of a group of proteins with a strongly conserved bicopper active centre able to bind molecular oxygen.
Christopher A Ramsden
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Systematic and Applied Microbiology, 2006
Tyrosinases are nearly ubiquitously distributed in all domains of life. They are essential for pigmentation and are important factors in wound healing and primary immune response. Their active site is characterized by a pair of antiferromagnetically coupled copper ions, CuA and CuB, which are coordinated by six histidine residues. Such a "type 3 copper
Harald, Claus, Heinz, Decker
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Tyrosinases are nearly ubiquitously distributed in all domains of life. They are essential for pigmentation and are important factors in wound healing and primary immune response. Their active site is characterized by a pair of antiferromagnetically coupled copper ions, CuA and CuB, which are coordinated by six histidine residues. Such a "type 3 copper
Harald, Claus, Heinz, Decker
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Archives for Dermatological Research, 1975
Purified tyrosinase T1 was incubated with neuraminidase. The catalytic activity of tyrosinase was essentially retained, after this treatment. The tyrosinase band (Dopa stained) was transformed into a new less anodic form, similar to tyrosinase T2, on disc electrophoresis.
K, Miyazaki, N, Otaki
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Purified tyrosinase T1 was incubated with neuraminidase. The catalytic activity of tyrosinase was essentially retained, after this treatment. The tyrosinase band (Dopa stained) was transformed into a new less anodic form, similar to tyrosinase T2, on disc electrophoresis.
K, Miyazaki, N, Otaki
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Tyrosinase and Tyrosinase Inhibitors
Journal of Biocatalysis & Biotransformation, 2012Tyrosinase and Tyrosinase Inhibitors Melanin is responsible for skin color and plays an important role in protection of the skin against UV light induced damage. During the melanin biosynthesis pathway, tyrosinase (EC 1.14.18.1) is the rate-limiting enzyme that hydroxylates L-tyrosine to L-3,4- dihydroxyphenylalanine (L-DOPA), and L-DOPA is further ...
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Archives of Biochemistry and Biophysics, 1955
Abstract The inhibition of tyrosinase by halide salts and carboxylic acids has been studied at several pH values. The presence of the benzene nucleus complements the inhibitory characteristics of carboxylic acids, and the existence of a negatively charged group on the inhibitor is also shown to be a factor.
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Abstract The inhibition of tyrosinase by halide salts and carboxylic acids has been studied at several pH values. The presence of the benzene nucleus complements the inhibitory characteristics of carboxylic acids, and the existence of a negatively charged group on the inhibitor is also shown to be a factor.
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Biomedical applications of tyrosinases and tyrosinase inhibitors
Tyrosinase is involved in several human diseases, among which hypopigmentation and depigmentation conditions (vitiligo, idiopathic guttate hypomelanosis, pityriasis versicolor, pityriasis alba) and hyperpigmentations (melasma, lentigines, post-inflammatory and periorbital hyperpigmentation, cervical idiopathic poikiloderma and acanthosis nigricans ...Luigi, Pisano +2 more
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