http://purl.uniprot.org/citations/15208312 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/15208312 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/15208312 | http://www.w3.org/2000/01/rdf-schema#comment | "dUTPase is essential to keep uracil out of DNA. Crystal structures of substrate (dUTP and alpha,beta-imino-dUTP) and product complexes of wild type and mutant dUTPases were determined to reveal how an enzyme responsible for DNA integrity functions. A kinetic analysis of wild type and mutant dUTPases was performed to obtain relevant mechanistic information in solution. Substrate hydrolysis is shown to be initiated via in-line nucleophile attack of a water molecule oriented by an activating conserved aspartate residue. Substrate binding in a catalytically competent conformation is achieved by (i) multiple interactions of the triphosphate moiety with catalysis-assisting Mg2+, (ii) a concerted motion of residues from three conserved enzyme motifs as compared with the apoenzyme, and (iii) an intricate hydrogen-bonding network that includes several water molecules in the active site. Results provide an understanding for the catalytic role of conserved residues in dUTPases."xsd:string |
http://purl.uniprot.org/citations/15208312 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m406135200"xsd:string |
http://purl.uniprot.org/citations/15208312 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m406135200"xsd:string |
http://purl.uniprot.org/citations/15208312 | http://purl.uniprot.org/core/author | "Wilmanns M."xsd:string |
http://purl.uniprot.org/citations/15208312 | http://purl.uniprot.org/core/author | "Wilmanns M."xsd:string |
http://purl.uniprot.org/citations/15208312 | http://purl.uniprot.org/core/author | "Barabas O."xsd:string |
http://purl.uniprot.org/citations/15208312 | http://purl.uniprot.org/core/author | "Barabas O."xsd:string |
http://purl.uniprot.org/citations/15208312 | http://purl.uniprot.org/core/author | "Vertessy B.G."xsd:string |
http://purl.uniprot.org/citations/15208312 | http://purl.uniprot.org/core/author | "Vertessy B.G."xsd:string |
http://purl.uniprot.org/citations/15208312 | http://purl.uniprot.org/core/author | "Kovari J."xsd:string |
http://purl.uniprot.org/citations/15208312 | http://purl.uniprot.org/core/author | "Kovari J."xsd:string |
http://purl.uniprot.org/citations/15208312 | http://purl.uniprot.org/core/author | "Pongracz V."xsd:string |
http://purl.uniprot.org/citations/15208312 | http://purl.uniprot.org/core/author | "Pongracz V."xsd:string |
http://purl.uniprot.org/citations/15208312 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
http://purl.uniprot.org/citations/15208312 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
http://purl.uniprot.org/citations/15208312 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/15208312 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/15208312 | http://purl.uniprot.org/core/pages | "42907-42915"xsd:string |
http://purl.uniprot.org/citations/15208312 | http://purl.uniprot.org/core/pages | "42907-42915"xsd:string |
http://purl.uniprot.org/citations/15208312 | http://purl.uniprot.org/core/title | "Structural insights into the catalytic mechanism of phosphate ester hydrolysis by dUTPase."xsd:string |
http://purl.uniprot.org/citations/15208312 | http://purl.uniprot.org/core/title | "Structural insights into the catalytic mechanism of phosphate ester hydrolysis by dUTPase."xsd:string |
http://purl.uniprot.org/citations/15208312 | http://purl.uniprot.org/core/volume | "279"xsd:string |
http://purl.uniprot.org/citations/15208312 | http://purl.uniprot.org/core/volume | "279"xsd:string |