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http://purl.uniprot.org/citations/11839745http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11839745http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11839745http://www.w3.org/2000/01/rdf-schema#comment"The structure of the rat liver aflatoxin dialdehyde reductase (AKR7A1) has been solved to 1.38-A resolution. Although it shares a similar alpha/beta-barrel structure with other members of the aldo-keto reductase superfamily, AKR7A1 is the first dimeric member to be crystallized. The crystal structure also reveals details of the ternary complex as one subunit of the dimer contains NADP(+) and the inhibitor citrate. Although the underlying catalytic mechanism appears similar to other aldo-keto reductases, the substrate-binding pocket contains several charged amino acids (Arg-231 and Arg-327) that distinguish it from previously characterized aldo-keto reductases with respect to size and charge. These differences account for the substrate specificity for 4-carbon acid-aldehydes such as succinic semialdehyde and 2-carboxybenzaldehyde as well as for the idiosyncratic substrate aflatoxin B(1) dialdehyde of this subfamily of enzymes. Structural differences between the AKR7A1 ternary complex and apoenzyme reveal a significant hinged movement of the enzyme involving not only the loops of the structure but also parts of the alpha/beta-barrel most intimately involved in cofactor binding."xsd:string
http://purl.uniprot.org/citations/11839745http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m110808200"xsd:string
http://purl.uniprot.org/citations/11839745http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m110808200"xsd:string
http://purl.uniprot.org/citations/11839745http://purl.uniprot.org/core/author"Lapthorn A.J."xsd:string
http://purl.uniprot.org/citations/11839745http://purl.uniprot.org/core/author"Lapthorn A.J."xsd:string
http://purl.uniprot.org/citations/11839745http://purl.uniprot.org/core/author"Brown E."xsd:string
http://purl.uniprot.org/citations/11839745http://purl.uniprot.org/core/author"Brown E."xsd:string
http://purl.uniprot.org/citations/11839745http://purl.uniprot.org/core/author"Ellis E.M."xsd:string
http://purl.uniprot.org/citations/11839745http://purl.uniprot.org/core/author"Ellis E.M."xsd:string
http://purl.uniprot.org/citations/11839745http://purl.uniprot.org/core/author"Kozma E."xsd:string
http://purl.uniprot.org/citations/11839745http://purl.uniprot.org/core/author"Kozma E."xsd:string
http://purl.uniprot.org/citations/11839745http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11839745http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11839745http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11839745http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11839745http://purl.uniprot.org/core/pages"16285-16293"xsd:string
http://purl.uniprot.org/citations/11839745http://purl.uniprot.org/core/pages"16285-16293"xsd:string
http://purl.uniprot.org/citations/11839745http://purl.uniprot.org/core/title"The crystal structure of rat liver AKR7A1. A dimeric member of the aldo-keto reductase superfamily."xsd:string
http://purl.uniprot.org/citations/11839745http://purl.uniprot.org/core/title"The crystal structure of rat liver AKR7A1. A dimeric member of the aldo-keto reductase superfamily."xsd:string
http://purl.uniprot.org/citations/11839745http://purl.uniprot.org/core/volume"277"xsd:string
http://purl.uniprot.org/citations/11839745http://purl.uniprot.org/core/volume"277"xsd:string
http://purl.uniprot.org/citations/11839745http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11839745
http://purl.uniprot.org/citations/11839745http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11839745