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http://purl.uniprot.org/citations/1730675http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1730675http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1730675http://www.w3.org/2000/01/rdf-schema#comment"Pyrroline-5-carboxylate reductase (EC 1.5.1.2) catalyzes the NAD(P)H-dependent conversion of pyrroline-5-carboxylate to proline. We cloned a human pyrroline-5-carboxylate reductase cDNA by complementation of proline auxotrophy in a Saccharomyces cerevisiae mutant strain, DT1100. Using a HepG2 cDNA library in a yeast expression vector, we screened 10(5) transformants, two of which gained proline prototrophy. The plasmids in both contained similar 1.8-kilobase inserts, which when reintroduced into strain DT1100, conferred proline prototrophy. The pyrroline-5-carboxylate reductase activity in these prototrophs was 1-3% that of wild type yeast, in contrast to the activity in strain DT1100 which was undetectable. The 1810-base pair pyrroline-5-carboxylate reductase cDNA hybridizes to a 1.85-kilobase mRNA in samples from human cell lines and predicts a 319-amino acid, 33.4-kDa protein. The derived amino acid sequence is 32% identical with that of S. cerevisiae. By genomic DNA hybridization analysis, the human reductase appears to be encoded by a single copy gene which maps to chromosome 17."xsd:string
http://purl.uniprot.org/citations/1730675http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(18)48364-0"xsd:string
http://purl.uniprot.org/citations/1730675http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(18)48364-0"xsd:string
http://purl.uniprot.org/citations/1730675http://purl.uniprot.org/core/author"Valle D."xsd:string
http://purl.uniprot.org/citations/1730675http://purl.uniprot.org/core/author"Valle D."xsd:string
http://purl.uniprot.org/citations/1730675http://purl.uniprot.org/core/author"Brandriss M.C."xsd:string
http://purl.uniprot.org/citations/1730675http://purl.uniprot.org/core/author"Brandriss M.C."xsd:string
http://purl.uniprot.org/citations/1730675http://purl.uniprot.org/core/author"Dougherty K.M."xsd:string
http://purl.uniprot.org/citations/1730675http://purl.uniprot.org/core/author"Dougherty K.M."xsd:string
http://purl.uniprot.org/citations/1730675http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1730675http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1730675http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/1730675http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/1730675http://purl.uniprot.org/core/pages"871-875"xsd:string
http://purl.uniprot.org/citations/1730675http://purl.uniprot.org/core/pages"871-875"xsd:string
http://purl.uniprot.org/citations/1730675http://purl.uniprot.org/core/title"Cloning human pyrroline-5-carboxylate reductase cDNA by complementation in Saccharomyces cerevisiae."xsd:string
http://purl.uniprot.org/citations/1730675http://purl.uniprot.org/core/title"Cloning human pyrroline-5-carboxylate reductase cDNA by complementation in Saccharomyces cerevisiae."xsd:string
http://purl.uniprot.org/citations/1730675http://purl.uniprot.org/core/volume"267"xsd:string
http://purl.uniprot.org/citations/1730675http://purl.uniprot.org/core/volume"267"xsd:string
http://purl.uniprot.org/citations/1730675http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1730675
http://purl.uniprot.org/citations/1730675http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1730675
http://purl.uniprot.org/citations/1730675http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/1730675
http://purl.uniprot.org/citations/1730675http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/1730675