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http://purl.uniprot.org/citations/9032445http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9032445http://www.w3.org/2000/01/rdf-schema#comment"Simultaneous multiple alignment of available sequences of the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase revealed several segments of conserved residues in the 2-kinase domain. The sequence of the kinase domain was also compared with proteins of known three-dimensional structure. No similarity was found between the kinase domain of 6-phosphofructo-2-kinase and 6-phosphofructo-1-kinase. This questions the modelling of the 2-kinase domain on bacterial 6-phosphofructo-1-kinase that has previously been proposed [Bazan, Fletterick and Pilkis (1989) Proc. Natl. Acad. Sci. U.S.A. 86, 9642-9646]. However, sequence similarities were found between the 2-kinase domain and several nucleotide-binding proteins, the most similar being adenylate kinase. A structural model of the 2-kinase domain based on adenylate kinase is proposed. It accommodates all the results of site-directed mutagenesis studies carried out to date on residues in the 2-kinase domain. It also allows residues potentially involved in catalysis and/or substrate binding to be predicted."xsd:string
http://purl.uniprot.org/citations/9032445http://purl.org/dc/terms/identifier"doi:10.1042/bj3210615"xsd:string
http://purl.uniprot.org/citations/9032445http://purl.uniprot.org/core/author"Rider M.H."xsd:string
http://purl.uniprot.org/citations/9032445http://purl.uniprot.org/core/author"Vertommen D."xsd:string
http://purl.uniprot.org/citations/9032445http://purl.uniprot.org/core/author"Bertrand L."xsd:string
http://purl.uniprot.org/citations/9032445http://purl.uniprot.org/core/author"Hue L."xsd:string
http://purl.uniprot.org/citations/9032445http://purl.uniprot.org/core/author"Depiereux E."xsd:string
http://purl.uniprot.org/citations/9032445http://purl.uniprot.org/core/author"Feytmans E."xsd:string
http://purl.uniprot.org/citations/9032445http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9032445http://purl.uniprot.org/core/name"Biochem J"xsd:string
http://purl.uniprot.org/citations/9032445http://purl.uniprot.org/core/pages"615-621"xsd:string
http://purl.uniprot.org/citations/9032445http://purl.uniprot.org/core/title"Modelling the 2-kinase domain of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase on adenylate kinase."xsd:string
http://purl.uniprot.org/citations/9032445http://purl.uniprot.org/core/volume"321"xsd:string
http://purl.uniprot.org/citations/9032445http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9032445
http://purl.uniprot.org/citations/9032445http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9032445
http://purl.uniprot.org/uniprot/#_P32604-mappedCitation-9032445http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/9032445
http://purl.uniprot.org/uniprot/P32604http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/9032445