Abstract
A mutant ofEscherichia coli K-12, originally though to lack the major murein lipoprotein (product of the1pp gene) was found to contain an intact1pp locus and to exhibit multiple physiological defects. These included altered morphology, sensitivity to glycine, sensitivity to high temperature, and absolute requirement for certain vitamin B6 derivatives. The genetic properties of the mutant indicated that a chromosomal inversion had caused inactivation of thepdxH (pyridoxine phosphate oxidase) gene. Behavior of this and other Pdx− mutants indicated that growth in unsupplemented complex medium can lead to pyridoxal phosphate limitation and concomitant impairment of cell wall biosynthesis.
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