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http://purl.uniprot.org/citations/8527927http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8527927http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8527927http://www.w3.org/2000/01/rdf-schema#comment"2'-Deoxyuridylate hydroxymethylase (dUMP-hmase) from phage SPO1 has been cloned and expressed in Escherichia coli. In crude extracts, the enzyme represents about 25% of the soluble protein and has a higher specific activity than the most purified preparation yet reported. The enzyme was purified to homogeneity by ion-exchange and hydrophobic chromatography. The subunits of dUMP-hmase are 45 kDa by SDS-PAGE and form dimers with a molecular mass of 89.2 kDa by analytical centrifugation. In addition to the normal reaction, dUMP-hmase catalyzes the 5,10-methylene-5,6,7,8-tetrahydrofolate (CH2H4folate)-independent tritium exchange of [5-3H]dUMP for protons of water and dehalogenation of 5-bromo-2'-deoxy-uridine-5'-monophosphate; the enzyme also forms a covalent binary adduct with pyridoxal 5'-monophosphate and a covalent ternary complex with 5-fluoro-2'-deoxyuridine-5'-monophosphate and CH2H4folate. Folic acid inhibits the tritium release catalyzed by dUMP-hmase in the presence of cofactor but has no effect on the catalysis of cofactor-independent tritium exchange."xsd:string
http://purl.uniprot.org/citations/8527927http://purl.org/dc/terms/identifier"doi:10.1006/prep.1995.1057"xsd:string
http://purl.uniprot.org/citations/8527927http://purl.org/dc/terms/identifier"doi:10.1006/prep.1995.1057"xsd:string
http://purl.uniprot.org/citations/8527927http://purl.uniprot.org/core/author"Santi D.V."xsd:string
http://purl.uniprot.org/citations/8527927http://purl.uniprot.org/core/author"Santi D.V."xsd:string
http://purl.uniprot.org/citations/8527927http://purl.uniprot.org/core/author"Livi L.L."xsd:string
http://purl.uniprot.org/citations/8527927http://purl.uniprot.org/core/author"Livi L.L."xsd:string
http://purl.uniprot.org/citations/8527927http://purl.uniprot.org/core/author"Schellenberger U."xsd:string
http://purl.uniprot.org/citations/8527927http://purl.uniprot.org/core/author"Schellenberger U."xsd:string
http://purl.uniprot.org/citations/8527927http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/8527927http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/8527927http://purl.uniprot.org/core/name"Protein Expr. Purif."xsd:string
http://purl.uniprot.org/citations/8527927http://purl.uniprot.org/core/name"Protein Expr. Purif."xsd:string
http://purl.uniprot.org/citations/8527927http://purl.uniprot.org/core/pages"423-430"xsd:string
http://purl.uniprot.org/citations/8527927http://purl.uniprot.org/core/pages"423-430"xsd:string
http://purl.uniprot.org/citations/8527927http://purl.uniprot.org/core/title"Cloning, expression, purification, and characterization of 2'-deoxyuridylate hydroxymethylase from phage SPO1."xsd:string
http://purl.uniprot.org/citations/8527927http://purl.uniprot.org/core/title"Cloning, expression, purification, and characterization of 2'-deoxyuridylate hydroxymethylase from phage SPO1."xsd:string
http://purl.uniprot.org/citations/8527927http://purl.uniprot.org/core/volume"6"xsd:string
http://purl.uniprot.org/citations/8527927http://purl.uniprot.org/core/volume"6"xsd:string
http://purl.uniprot.org/citations/8527927http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8527927
http://purl.uniprot.org/citations/8527927http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8527927
http://purl.uniprot.org/citations/8527927http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8527927
http://purl.uniprot.org/citations/8527927http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8527927