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http://purl.uniprot.org/citations/12200544http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12200544http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12200544http://www.w3.org/2000/01/rdf-schema#comment"Sequence analysis of a cDNA for D-erythrulose reductase from chicken liver showed that the deduced open reading frame encodes the protein with a molecular mass of 26 kDa consisting of 246 amino acids. Although the reductase shares more than 60% identity in the amino acid sequence with the mouse tetrameric carbonyl reductase, these two enzymes have many biochemical differences; their substrate specificity, subcellular localization, organ distribution, etc. A three-dimensional structure of D-erythrulose reductase was predicted by comparative modeling based on the structure of the tetrameric carbonyl reductase (PDB entry = 1CYD). Most of the residues at the active site (within 4 A from the ligand) of the carbonyl reductase were also conserved in the D-erythrulose reductase. Nevertheless, Val190 and Leu146 in the active site of the tetrameric carbonyl reductase were substituted in the D-erythrulose reductase by Asn192 and His148, respectively. The substitutions in the active sites may be related to the difference in substrate specificity of the two enzymes. The phylogenic analysis of D-erythrulose reductase and the other related proteins suggests that the protein described as a carbonyl reductase D-erythrulose reductase."xsd:string
http://purl.uniprot.org/citations/12200544http://purl.org/dc/terms/identifier"doi:10.1093/protein/15.7.611"xsd:string
http://purl.uniprot.org/citations/12200544http://purl.org/dc/terms/identifier"doi:10.1093/protein/15.7.611"xsd:string
http://purl.uniprot.org/citations/12200544http://purl.uniprot.org/core/author"Kaku H."xsd:string
http://purl.uniprot.org/citations/12200544http://purl.uniprot.org/core/author"Kaku H."xsd:string
http://purl.uniprot.org/citations/12200544http://purl.uniprot.org/core/author"Maeda M."xsd:string
http://purl.uniprot.org/citations/12200544http://purl.uniprot.org/core/author"Maeda M."xsd:string
http://purl.uniprot.org/citations/12200544http://purl.uniprot.org/core/author"Shimada M."xsd:string
http://purl.uniprot.org/citations/12200544http://purl.uniprot.org/core/author"Shimada M."xsd:string
http://purl.uniprot.org/citations/12200544http://purl.uniprot.org/core/author"Nishioka T."xsd:string
http://purl.uniprot.org/citations/12200544http://purl.uniprot.org/core/author"Nishioka T."xsd:string
http://purl.uniprot.org/citations/12200544http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12200544http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12200544http://purl.uniprot.org/core/name"Protein Eng."xsd:string
http://purl.uniprot.org/citations/12200544http://purl.uniprot.org/core/name"Protein Eng."xsd:string
http://purl.uniprot.org/citations/12200544http://purl.uniprot.org/core/pages"611-617"xsd:string
http://purl.uniprot.org/citations/12200544http://purl.uniprot.org/core/pages"611-617"xsd:string
http://purl.uniprot.org/citations/12200544http://purl.uniprot.org/core/title"Cloning and sequence analysis of D-erythrulose reductase from chicken: its close structural relation to tetrameric carbonyl reductases."xsd:string
http://purl.uniprot.org/citations/12200544http://purl.uniprot.org/core/title"Cloning and sequence analysis of D-erythrulose reductase from chicken: its close structural relation to tetrameric carbonyl reductases."xsd:string
http://purl.uniprot.org/citations/12200544http://purl.uniprot.org/core/volume"15"xsd:string
http://purl.uniprot.org/citations/12200544http://purl.uniprot.org/core/volume"15"xsd:string
http://purl.uniprot.org/citations/12200544http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12200544
http://purl.uniprot.org/citations/12200544http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12200544