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http://purl.uniprot.org/citations/12730263http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12730263http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12730263http://www.w3.org/2000/01/rdf-schema#comment"The glycine-serine interconversion, catalysed by glycine decarboxylase and serine hydroxymethyltransferase, is an important reaction of primary metabolism in all organisms including plants, by providing one-carbon units for many biosynthetic reactions. In plants, in addition, it is an integral part of the photorespiratory metabolic pathway and produces large amounts of photorespiratory CO(2) within mitochondria. Although controversial, there is significant evidence that this process, by the relocation of glycine decarboxylase within the leaves from the mesophyll to the bundle-sheath, contributed to the evolution of C(4) photosynthesis. In this review, some aspects of current knowledge about glycine decarboxylase and serine hydroxymethyltransferase and the role of these enzymes in metabolism, about the corresponding genes and their expression as well as about mutants and anti-sense plants related to these genes or processes will be summarized and discussed. From a comparison of the available information about the number and organization of GDC and SHMT genes in the genomes of Arabidopsis thaliana and Oryza sativa it appears that these and, possibly, other genes related to photorespiration, are similarly organized even in only very distantly related angiosperms."xsd:string
http://purl.uniprot.org/citations/12730263http://purl.org/dc/terms/identifier"doi:10.1093/jxb/erg171"xsd:string
http://purl.uniprot.org/citations/12730263http://purl.org/dc/terms/identifier"doi:10.1093/jxb/erg171"xsd:string
http://purl.uniprot.org/citations/12730263http://purl.uniprot.org/core/author"Kolukisaoglu U."xsd:string
http://purl.uniprot.org/citations/12730263http://purl.uniprot.org/core/author"Kolukisaoglu U."xsd:string
http://purl.uniprot.org/citations/12730263http://purl.uniprot.org/core/author"Bauwe H."xsd:string
http://purl.uniprot.org/citations/12730263http://purl.uniprot.org/core/author"Bauwe H."xsd:string
http://purl.uniprot.org/citations/12730263http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12730263http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12730263http://purl.uniprot.org/core/name"J. Exp. Bot."xsd:string
http://purl.uniprot.org/citations/12730263http://purl.uniprot.org/core/name"J. Exp. Bot."xsd:string
http://purl.uniprot.org/citations/12730263http://purl.uniprot.org/core/pages"1523-1535"xsd:string
http://purl.uniprot.org/citations/12730263http://purl.uniprot.org/core/pages"1523-1535"xsd:string
http://purl.uniprot.org/citations/12730263http://purl.uniprot.org/core/title"Genetic manipulation of glycine decarboxylation."xsd:string
http://purl.uniprot.org/citations/12730263http://purl.uniprot.org/core/title"Genetic manipulation of glycine decarboxylation."xsd:string
http://purl.uniprot.org/citations/12730263http://purl.uniprot.org/core/volume"54"xsd:string
http://purl.uniprot.org/citations/12730263http://purl.uniprot.org/core/volume"54"xsd:string
http://purl.uniprot.org/citations/12730263http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12730263
http://purl.uniprot.org/citations/12730263http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12730263
http://purl.uniprot.org/citations/12730263http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12730263
http://purl.uniprot.org/citations/12730263http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12730263
http://purl.uniprot.org/uniprot/Q9SZJ5http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/12730263
http://purl.uniprot.org/uniprot/Q94B78http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/12730263