title: Characterization of pyridoxine auxotrophs of Escherichia coli: serine and pdxF mutants.
abstract: At least six phenotypically distinct classes of mutants of Escherichia coli which require serine or pyridoxine or both can be isolated. Three of the six classes lack 3-phosphoserine-2-oxoglutarate aminotransferase. One of these classes contains WG5, a mutant previously characterized as containing the pdxF5 allele. The aminotransferase isolated from this mutant has been compared to that isolated from wild-type E. coli and found to have apparently normal affinity for pyridoxal 5'-phosphate, but reduced affinity for pyridoxamine 5'-phosphate.
mesh_terms: D003470:Culture Media; D003720:Densitometry; D004926:Escherichia coli / Q000187:drug effects / Q000201:enzymology / Q000254:growth & development / Q000378:metabolism*; D005827:Genetics, Microbial; D005993:Glycerolphosphate Dehydrogenase / Q000378:metabolism; D009154:Mutation; D010641:Phenotype; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism; D011732:Pyridoxal Phosphate / Q000494:pharmacology; D011736:Pyridoxine / Q000096:biosynthesis / Q000378:metabolism*; D012694:Serine / Q000378:metabolism* / Q000494:pharmacology; D000637:Transaminases / Q000378:metabolism
chemical_list: D003470:Culture Media; D012694:Serine; D011732:Pyridoxal Phosphate; D005993:Glycerolphosphate Dehydrogenase; D000637:Transaminases; D010744:Phosphoric Monoester Hydrolases; D011736:Pyridoxine