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Abstract
SUMMARY: Mutants of Escherichia coli K12 blocked in the oxidation of pyridoxine 5′-phosphate (‘Oxidase’ mutants) excreted pyridoxine at an initial rate of 19 pmol h−1 (108 bacteria)−1, i.e. 0·6 nmol h−1 (mg dry wt)−1, when starved for pyridoxal. Glycolaldehyde, l-phosphoserine, dl-serine and, to a lesser extent, l-leucine stimulated the rate of pyridoxine excretion, but there was no significant stimulation by 2′-hydroxypyridoxine. 4′-Deoxypyridoxine inhibited or stimulated growth of the ‘Oxidase’ mutant, depending on the relative concentrations of added pyridoxal and 4′-deoxypyridoxine. It was concluded that stimulation of growth by 4′-deoxypyridoxine was due to its conversion to pyridoxal.
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© Society for General Microbiology, 1979