| http://purl.uniprot.org/citations/15247385 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15247385 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15247385 | http://www.w3.org/2000/01/rdf-schema#comment | "Pectic cell wall polysaccharides owe their high negative charge to the presence of D-galacturonate, a monosaccharide that appears to be present only in plants and some prokaryotes. UDP-D-galacturonate, the activated form of this sugar, is known to be formed by the 4-epimerization of UDP-D-glucuronate; however, no coding regions for the epimerase catalyzing this reaction have previously been described in plants. To better understand the mechanisms by which precursors for pectin synthesis are produced, we used a bioinformatics approach to identify and functionally express a UDP-D-glucuronate 4-epimerase (GAE1) from Arabidopsis. GAE1 is predicted to be a type II membrane protein that belongs to the family of short-chain dehydrogenases/reductases. The recombinant enzyme expressed in Pichia pastoris established a 1.3:1 equilibrium between UDP-D-galacturonate and UDP-D-glucuronate but did not epimerize UDP-D-Glc or UDP-D-Xyl. Enzyme assays on cell extracts localized total UDP-D-glucuronate 4-epimerase and recombinant GAE1 activity exclusively to the microsomal fractions of Arabidopsis and Pichia, respectively. GAE1 had a pH optimum of 7.6 and an apparent Km of 0.19 mm. The recombinant enzyme was strongly inhibited by UDP-D-Xyl but not by UDP, UDP-D-Glc, or UDP-D-Gal. Analysis of Arabidopsis plants transformed with a GAE1:GUS construct showed expression in all tissues. The Arabidopsis genome contains five GAE1 paralogs, all of which are transcribed and predicted to contain a membrane anchor. This suggests that all of these enzymes are targeted to an endomembrane system such as the Golgi where they may provide UDP-D-galacturonate to glycosyltransferases in pectin synthesis."xsd:string |
| http://purl.uniprot.org/citations/15247385 | http://purl.org/dc/terms/identifier | "doi:10.1104/pp.104.043745"xsd:string |
| http://purl.uniprot.org/citations/15247385 | http://purl.org/dc/terms/identifier | "doi:10.1104/pp.104.043745"xsd:string |
| http://purl.uniprot.org/citations/15247385 | http://purl.uniprot.org/core/author | "Reiter W.-D."xsd:string |
| http://purl.uniprot.org/citations/15247385 | http://purl.uniprot.org/core/author | "Reiter W.-D."xsd:string |
| http://purl.uniprot.org/citations/15247385 | http://purl.uniprot.org/core/author | "Moelhoej M."xsd:string |
| http://purl.uniprot.org/citations/15247385 | http://purl.uniprot.org/core/author | "Moelhoej M."xsd:string |
| http://purl.uniprot.org/citations/15247385 | http://purl.uniprot.org/core/author | "Verma R."xsd:string |
| http://purl.uniprot.org/citations/15247385 | http://purl.uniprot.org/core/author | "Verma R."xsd:string |
| http://purl.uniprot.org/citations/15247385 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15247385 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15247385 | http://purl.uniprot.org/core/name | "Plant Physiol."xsd:string |
| http://purl.uniprot.org/citations/15247385 | http://purl.uniprot.org/core/name | "Plant Physiol."xsd:string |
| http://purl.uniprot.org/citations/15247385 | http://purl.uniprot.org/core/pages | "1221-1230"xsd:string |
| http://purl.uniprot.org/citations/15247385 | http://purl.uniprot.org/core/pages | "1221-1230"xsd:string |
| http://purl.uniprot.org/citations/15247385 | http://purl.uniprot.org/core/title | "The biosynthesis of D-galacturonate in plants. Functional cloning and characterization of a membrane-anchored UDP-D-glucuronate 4-epimerase from Arabidopsis."xsd:string |
| http://purl.uniprot.org/citations/15247385 | http://purl.uniprot.org/core/title | "The biosynthesis of D-galacturonate in plants. Functional cloning and characterization of a membrane-anchored UDP-D-glucuronate 4-epimerase from Arabidopsis."xsd:string |
| http://purl.uniprot.org/citations/15247385 | http://purl.uniprot.org/core/volume | "135"xsd:string |
| http://purl.uniprot.org/citations/15247385 | http://purl.uniprot.org/core/volume | "135"xsd:string |
| http://purl.uniprot.org/citations/15247385 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15247385 |
| http://purl.uniprot.org/citations/15247385 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15247385 |
| http://purl.uniprot.org/citations/15247385 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15247385 |
| http://purl.uniprot.org/citations/15247385 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15247385 |