| http://purl.uniprot.org/citations/8595869 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8595869 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8595869 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/8595869 | http://www.w3.org/2000/01/rdf-schema#comment | "We show that thrB-encoded homoserine kinase is required for growth of Escherichia coli K-12 pdxB mutants on minimal glucose medium supplemented with 4-hydroxy-L-threonine (synonym, 3-hydroxyhomoserine) or D-glycolaldehyde. This result is consistent with a model in which 4-phospho-hydroxy-L-threonine (synonym, 3-hydroxyhomoserine phosphate), rather than 4-hydroxy-L-threonine, is an obligatory intermediate in pyridoxal 5'-phosphate biosynthesis. Ring closure using 4-phospho-hydroxy-L-threonine as a substrate would lead to formation of pyridoxine 5'-phosphate, and not pyridoxine, as the first B6-vitamer synthesized de novo. These considerations suggest that E. coli pyridoxal/pyridoxamine/pyridoxine kinase is not required for the main de novo pathway of pyridoxal 5'-phosphate biosynthesis, and instead plays a role only in the B6-vitamer salvage pathway."xsd:string |
| http://purl.uniprot.org/citations/8595869 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1574-6968.1996.tb08001.x"xsd:string |
| http://purl.uniprot.org/citations/8595869 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1574-6968.1996.tb08001.x"xsd:string |
| http://purl.uniprot.org/citations/8595869 | http://purl.uniprot.org/core/author | "Zhao G."xsd:string |
| http://purl.uniprot.org/citations/8595869 | http://purl.uniprot.org/core/author | "Zhao G."xsd:string |
| http://purl.uniprot.org/citations/8595869 | http://purl.uniprot.org/core/author | "Winkler M.E."xsd:string |
| http://purl.uniprot.org/citations/8595869 | http://purl.uniprot.org/core/author | "Winkler M.E."xsd:string |
| http://purl.uniprot.org/citations/8595869 | http://purl.uniprot.org/core/date | "1996"xsd:gYear |
| http://purl.uniprot.org/citations/8595869 | http://purl.uniprot.org/core/date | "1996"xsd:gYear |
| http://purl.uniprot.org/citations/8595869 | http://purl.uniprot.org/core/name | "FEMS Microbiol. Lett."xsd:string |
| http://purl.uniprot.org/citations/8595869 | http://purl.uniprot.org/core/name | "FEMS Microbiol. Lett."xsd:string |
| http://purl.uniprot.org/citations/8595869 | http://purl.uniprot.org/core/pages | "275-280"xsd:string |
| http://purl.uniprot.org/citations/8595869 | http://purl.uniprot.org/core/pages | "275-280"xsd:string |
| http://purl.uniprot.org/citations/8595869 | http://purl.uniprot.org/core/title | "4-phospho-hydroxy-L-threonine is an obligatory intermediate in pyridoxal 5'-phosphate coenzyme biosynthesis in Escherichia coli K-12."xsd:string |
| http://purl.uniprot.org/citations/8595869 | http://purl.uniprot.org/core/title | "4-phospho-hydroxy-L-threonine is an obligatory intermediate in pyridoxal 5'-phosphate coenzyme biosynthesis in Escherichia coli K-12."xsd:string |
| http://purl.uniprot.org/citations/8595869 | http://purl.uniprot.org/core/volume | "135"xsd:string |
| http://purl.uniprot.org/citations/8595869 | http://purl.uniprot.org/core/volume | "135"xsd:string |
| http://purl.uniprot.org/citations/8595869 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/8595869 |
| http://purl.uniprot.org/citations/8595869 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/8595869 |
| http://purl.uniprot.org/citations/8595869 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/8595869 |
| http://purl.uniprot.org/citations/8595869 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/8595869 |
| http://purl.uniprot.org/citations/8595869 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/8595869 |