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http://purl.uniprot.org/citations/1572351http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1572351http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1572351http://www.w3.org/2000/01/rdf-schema#comment"The primary structure of Pseudomonas 4-hydroxyphenylpyruvate dioxygenase was determined. Sequence degradation of the intact protein and of peptides from three different digests of the carboxymethylated protein established a 357-residue polypeptide chain with a free alpha-amino group. Hydroxylamine cleavage at a single Asn-Gly sequence was useful. Comparisons with known structures in data banks revealed no close relationship with other characterized proteins. The human enzyme has a related composition, suggesting that also the eukaryotic form belongs to this protein type, but with a blocked N-terminus like in many other eukaryotic intracellular proteins. Secondary structure predictions suggest an alpha/beta mixed structure, fairly typical of globular proteins, without long segments of hydrophobicity or charge, although a region in the middle of the C-terminal third of the subunit appears to have the most extreme properties. A ferric centre, correlating with enzyme activity and absorbance at 595 nm, has previously been assigned to tyrosinate coordination. The Tyr and His distributions, and the position of a single Cys residue, all suggest a few likely sites, outside the C-terminal segment, for this centre."xsd:string
http://purl.uniprot.org/citations/1572351http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1992.tb16800.x"xsd:string
http://purl.uniprot.org/citations/1572351http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1992.tb16800.x"xsd:string
http://purl.uniprot.org/citations/1572351http://purl.uniprot.org/core/author"Joernvall H."xsd:string
http://purl.uniprot.org/citations/1572351http://purl.uniprot.org/core/author"Joernvall H."xsd:string
http://purl.uniprot.org/citations/1572351http://purl.uniprot.org/core/author"Barros-Soederling J."xsd:string
http://purl.uniprot.org/citations/1572351http://purl.uniprot.org/core/author"Barros-Soederling J."xsd:string
http://purl.uniprot.org/citations/1572351http://purl.uniprot.org/core/author"Lindstedt S."xsd:string
http://purl.uniprot.org/citations/1572351http://purl.uniprot.org/core/author"Lindstedt S."xsd:string
http://purl.uniprot.org/citations/1572351http://purl.uniprot.org/core/author"Odelhoeg B."xsd:string
http://purl.uniprot.org/citations/1572351http://purl.uniprot.org/core/author"Odelhoeg B."xsd:string
http://purl.uniprot.org/citations/1572351http://purl.uniprot.org/core/author"Persson B."xsd:string
http://purl.uniprot.org/citations/1572351http://purl.uniprot.org/core/author"Persson B."xsd:string
http://purl.uniprot.org/citations/1572351http://purl.uniprot.org/core/author"Rueetschi U."xsd:string
http://purl.uniprot.org/citations/1572351http://purl.uniprot.org/core/author"Rueetschi U."xsd:string
http://purl.uniprot.org/citations/1572351http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1572351http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1572351http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/1572351http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/1572351http://purl.uniprot.org/core/pages"459-466"xsd:string
http://purl.uniprot.org/citations/1572351http://purl.uniprot.org/core/pages"459-466"xsd:string
http://purl.uniprot.org/citations/1572351http://purl.uniprot.org/core/title"Characterization of 4-hydroxyphenylpyruvate dioxygenase. Primary structure of the Pseudomonas enzyme."xsd:string
http://purl.uniprot.org/citations/1572351http://purl.uniprot.org/core/title"Characterization of 4-hydroxyphenylpyruvate dioxygenase. Primary structure of the Pseudomonas enzyme."xsd:string