Characterization of Pyridoxine Auxotrophs of Escherichia coli: Serine and PdxF Mutants
AUTOR(ES)
Dempsey, Walter B.
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=285042Documentos Relacionados
- Characterization of Pyridoxine Auxotrophs of Escherichia coli: P1 Transduction
- Characterization of Pyridoxine Auxotrophs of Escherichia coli: Chromosomal Position of Linkage Group I
- Pyridoxine-requiring mutants of Escherichia coli: glycolaldehyde dehydrogenase is not coded for by the pdxB gene.
- Isolation and Characterization of Pyridoxine Auxotrophs of Escherichia coli1
- Serine hydroxymethyltransferase from Escherichia coli: purification and properties.
