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http://purl.uniprot.org/citations/12514241http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12514241http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12514241http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/12514241http://www.w3.org/2000/01/rdf-schema#comment"P1-zeta-crystallin (P1-ZCr) is an oxidative stress-induced NADPH:quinone oxidoreductase in Arabidopsis thaliana, but its physiological electron acceptors have not been identified. We found that recombinant P1-ZCr catalyzed the reduction of 2-alkenals of carbon chain C(3)-C(9) with NADPH. Among these 2-alkenals, the highest specificity was observed for 4-hydroxy-(2E)-nonenal (HNE), one of the major toxic products generated from lipid peroxides. (3Z)-Hexenal and aldehydes without alpha,beta-unsaturated bonds did not serve as electron acceptors. In the 2-alkenal molecules, P1-ZCr catalyzed the hydrogenation of alpha,beta-unsaturated bonds, but not the reduction of the aldehyde moiety, to produce saturated aldehydes, as determined by gas chromatography/mass spectrometry. We propose the enzyme name NADPH:2-alkenal alpha,beta-hydrogenase (ALH). A major portion of the NADPH-dependent HNE-reducing activity in A. thaliana leaves was inhibited by the specific antiserum against P1-ZCr, indicating that the endogenous P1-ZCr protein has ALH activity. Because expression of the P1-ZCr gene in A. thaliana is induced by oxidative stress treatments, we conclude that P1-ZCr functions as a defense against oxidative stress by scavenging the highly toxic, lipid peroxide-derived alpha,beta-unsaturated aldehydes."xsd:string
http://purl.uniprot.org/citations/12514241http://purl.org/dc/terms/identifier"doi:10.1093/pcp/pcf187"xsd:string
http://purl.uniprot.org/citations/12514241http://purl.org/dc/terms/identifier"doi:10.1093/pcp/pcf187"xsd:string
http://purl.uniprot.org/citations/12514241http://purl.uniprot.org/core/author"Asada K."xsd:string
http://purl.uniprot.org/citations/12514241http://purl.uniprot.org/core/author"Asada K."xsd:string
http://purl.uniprot.org/citations/12514241http://purl.uniprot.org/core/author"Hayashi S."xsd:string
http://purl.uniprot.org/citations/12514241http://purl.uniprot.org/core/author"Hayashi S."xsd:string
http://purl.uniprot.org/citations/12514241http://purl.uniprot.org/core/author"Babiychuk E."xsd:string
http://purl.uniprot.org/citations/12514241http://purl.uniprot.org/core/author"Babiychuk E."xsd:string
http://purl.uniprot.org/citations/12514241http://purl.uniprot.org/core/author"Nakamura K."xsd:string
http://purl.uniprot.org/citations/12514241http://purl.uniprot.org/core/author"Nakamura K."xsd:string
http://purl.uniprot.org/citations/12514241http://purl.uniprot.org/core/author"Inze D."xsd:string
http://purl.uniprot.org/citations/12514241http://purl.uniprot.org/core/author"Inze D."xsd:string
http://purl.uniprot.org/citations/12514241http://purl.uniprot.org/core/author"Kushnir S."xsd:string
http://purl.uniprot.org/citations/12514241http://purl.uniprot.org/core/author"Kushnir S."xsd:string
http://purl.uniprot.org/citations/12514241http://purl.uniprot.org/core/author"Matsui K."xsd:string
http://purl.uniprot.org/citations/12514241http://purl.uniprot.org/core/author"Matsui K."xsd:string
http://purl.uniprot.org/citations/12514241http://purl.uniprot.org/core/author"Mano J."xsd:string
http://purl.uniprot.org/citations/12514241http://purl.uniprot.org/core/author"Mano J."xsd:string
http://purl.uniprot.org/citations/12514241http://purl.uniprot.org/core/author"Takimoto K."xsd:string
http://purl.uniprot.org/citations/12514241http://purl.uniprot.org/core/author"Takimoto K."xsd:string
http://purl.uniprot.org/citations/12514241http://purl.uniprot.org/core/author"Torii Y."xsd:string