Characterization of Pyridoxine Auxotrophs ofEscherichia coli: Serine and PdxF Mutants
Author(s) -
Walter B. Dempsey,
Hajime Itoh
Publication year - 1970
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.104.2.658-667.1970
Subject(s) - biology , escherichia coli , auxotrophy , mutant , pyridoxine , serine , pyridoxal , biochemistry , phosphoserine , pyridoxal phosphate , pyridoxamine , microbiology and biotechnology , phosphate , enzyme , gene , cofactor
At least six phenotypically distinct classes of mutants ofEscherichia 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 thepdxF5 allele. The aminotransferase isolated from this mutant has been compared to that isolated from wild-typeE. coli and found to have apparently normal affinity for pyridoxal 5′-phosphate, but reduced affinity for pyridoxamine 5′-phosphate.
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