PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 1898730-4 1991 By use of immune affinity purification protocols, we have isolated the proteins encoded by the brown and albino loci and have determined that both have the catalytic functions ascribed to tyrosinase, i.e. hydroxylation of tyrosine to 3,4-dihydroxyphenylalanine (DOPA) and the oxidation of DOPA to DOPAquinone. dopaquinone 297-308 tyrosinase Mus musculus 188-198 211676-2 1978 The inactivation similarly occurred in the dopa-tyrosinase reaction system containing ascorbic aicd, although in the presence of ascorbic acid the dopa-quinone is immediately converted back to dopa and therefore melanin formation does not take place. dopaquinone 147-159 tyrosinase Mus musculus 48-58 34088368-5 2021 Mechanically, the tyrosine groups on the surface of ECDY can be specifically recognized by tyrosinase and further converted into dopaquinone, which consequently causes the intramolecular fluorescence quenching of the probe through photoinduced electron transfer (PET). dopaquinone 129-140 tyrosinase Mus musculus 91-101 6413271-2 1983 The initial steps are the conversion of tyrosine to dihydroxyphenylalanine (dopa) and of dopa to dopaquinone by the enzyme tyrosinase (EC 1.10.3.1). dopaquinone 97-108 tyrosinase Mus musculus 123-133 6776205-3 1980 Tyrosinase inactivation also occurred when ascorbic acid was added to the reaction system; in which dopaquinone, an oxidation product of dopa which is immediately converted back to dopa by ascorbic acid thus preventing melanin formation. dopaquinone 100-111 tyrosinase Mus musculus 0-10 30579605-3 2019 Tyrosinase, a copper-containing protein, is the rate-limiting enzyme in melanin biosynthesis and first catalyzes the hydroxylation of l-tyrosine to 3,4-dihydroxyphenylalanine (DOPA) and the further oxidization to dopaquinone. dopaquinone 213-224 tyrosinase Mus musculus 0-10 26750991-2 2016 Tyrosinase, a type-3 copper protein, participates in two distinct reactions, hydroxylation of tyrosine to DOPA and conversion of DOPA to dopaquinone, in melanin biosynthesis. dopaquinone 137-148 tyrosinase Mus musculus 0-10 26544630-1 2015 Tyrosinase catalyzes two distinct sequential reactions in melanin biosynthesis: the hydroxylation of tyrosine to DOPA followed by the oxidation of DOPA to dopaquinone. dopaquinone 155-166 tyrosinase Mus musculus 0-10 26633377-1 2015 Tyrosinase catalyzes two distinct sequential reactions in melanin biosynthesis: The hydroxylation of tyrosine to dihydroxyphenylalanine (DOPA) and the oxidation of DOPA to dopaquinone. dopaquinone 172-183 tyrosinase Mus musculus 0-10 22110954-1 2010 Tyrosinase is a bifunctional enzyme which oxidizes the initial step of melanin biosynthesis, that is, conversion of tyrosine to dopa and subsequently dopa to dopaquinone. dopaquinone 158-169 tyrosinase Mus musculus 0-10 12878190-1 2003 Synthesis of melanin starts from the conversion of L-tyrosine to 3,4-dihydroxyphenylalanine (L-dopa) and then the oxidation of L-dopa yields dopaquinone by tyrosinase. dopaquinone 141-152 tyrosinase Mus musculus 156-166 19270393-5 2009 Additionally, the incubation of SH in mushroom tyrosinase inhibited the oxidation of l-dopa to o-dopaquinone, which implies that SH is a potent tyrosinase inhibitor. dopaquinone 95-108 tyrosinase Mus musculus 47-57 19270393-5 2009 Additionally, the incubation of SH in mushroom tyrosinase inhibited the oxidation of l-dopa to o-dopaquinone, which implies that SH is a potent tyrosinase inhibitor. dopaquinone 95-108 tyrosinase Mus musculus 144-154 8610070-2 1995 The melanin-affinic properties are apparently due to binding to intermediates, preferably dopaquinone, produced in the melanin synthetic pathway by tyrosinase-catalysed oxidation of tyrosine. dopaquinone 90-101 tyrosinase Mus musculus 148-158