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http://purl.uniprot.org/citations/1693779http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1693779http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1693779http://www.w3.org/2000/01/rdf-schema#comment"Melanogenesis is regulated in large part by tyrosinase (monophenol monooxygenase; monophenol, L-dopa:oxygen oxidoreductase, EC 1.14.18.1), and defective tyrosinase leads to albinism. The mechanisms for other pigmentation determinants (e.g., those operative in tyrosinase-positive albinism and in murine coat-color mutants) are not yet known. One murine pigmentation gene, the brown (b) locus, when mutated leads to a brown (b/b) or hypopigmented (Blt/Blt) coat versus the wild-type black (B/B). We show that the b locus codes for a glycoprotein with the activity of a catalase (hydrogen-peroxide:hydrogen-peroxide oxidoreductase, EC 1.11.1.6) (catalase B). Only the c locus protein is a tyrosinase. Because peroxides may be by-products of melanogenic activity and hydrogen peroxide in particular is known to destroy melanin precursors and melanin, we conclude that pigmentation is controlled not only by tyrosinase but also by a hydroperoxidase. Our studies indicate that catalase B is identical with gp75, a known human melanosomal glycoprotein; that the b mutation is in a heme-associated domain; and that the Blt mutation renders the protein susceptible to rapid proteolytic degradation."xsd:string
http://purl.uniprot.org/citations/1693779http://purl.org/dc/terms/identifier"doi:10.1073/pnas.87.12.4809"xsd:string
http://purl.uniprot.org/citations/1693779http://purl.org/dc/terms/identifier"doi:10.1073/pnas.87.12.4809"xsd:string
http://purl.uniprot.org/citations/1693779http://purl.uniprot.org/core/author"Halaban R."xsd:string
http://purl.uniprot.org/citations/1693779http://purl.uniprot.org/core/author"Halaban R."xsd:string
http://purl.uniprot.org/citations/1693779http://purl.uniprot.org/core/author"Moellmann G."xsd:string
http://purl.uniprot.org/citations/1693779http://purl.uniprot.org/core/author"Moellmann G."xsd:string
http://purl.uniprot.org/citations/1693779http://purl.uniprot.org/core/date"1990"xsd:gYear
http://purl.uniprot.org/citations/1693779http://purl.uniprot.org/core/date"1990"xsd:gYear
http://purl.uniprot.org/citations/1693779http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/1693779http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/1693779http://purl.uniprot.org/core/pages"4809-4813"xsd:string
http://purl.uniprot.org/citations/1693779http://purl.uniprot.org/core/pages"4809-4813"xsd:string
http://purl.uniprot.org/citations/1693779http://purl.uniprot.org/core/title"Murine and human b locus pigmentation genes encode a glycoprotein (gp75) with catalase activity."xsd:string
http://purl.uniprot.org/citations/1693779http://purl.uniprot.org/core/title"Murine and human b locus pigmentation genes encode a glycoprotein (gp75) with catalase activity."xsd:string
http://purl.uniprot.org/citations/1693779http://purl.uniprot.org/core/volume"87"xsd:string
http://purl.uniprot.org/citations/1693779http://purl.uniprot.org/core/volume"87"xsd:string
http://purl.uniprot.org/citations/1693779http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1693779
http://purl.uniprot.org/citations/1693779http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1693779
http://purl.uniprot.org/citations/1693779http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/1693779
http://purl.uniprot.org/citations/1693779http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/1693779
http://purl.uniprot.org/uniprot/P07147http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/1693779
http://purl.uniprot.org/uniprot/P17643http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/1693779