Isolation of a pdxJ point mutation that bypasses the requirement for the PdxH oxidase in pyridoxal 5' -phosphate coenzyme biosynthesis in Escherichia coli K-12

J Bacteriol. 1996 Apr;178(8):2445-9. doi: 10.1128/jb.178.8.2445-2449.1996.


We isolated 26 suppressor mutations that allowed growth of a delta pdxH::omega null mutant in the absence of pyridoxal. Each suppressor mapped to pdxJ, and the eight suppressors sequenced contained the same glycine-to-serine change in the PdxJ polypeptide. This bypass suppression suggests that PdxJ may participate in formation of the pyridine ring of pyridoxine 5'-phosphate.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Bacterial Proteins / genetics*
  • Escherichia coli / enzymology
  • Escherichia coli / genetics*
  • Escherichia coli Proteins*
  • Ligases*
  • Models, Biological
  • Mutagenesis, Insertional
  • Point Mutation*
  • Pyridoxal Phosphate / analogs & derivatives
  • Pyridoxal Phosphate / biosynthesis*
  • Pyridoxal Phosphate / metabolism
  • Pyridoxaminephosphate Oxidase / genetics
  • Pyridoxaminephosphate Oxidase / metabolism
  • Sequence Deletion
  • Suppression, Genetic*


  • Bacterial Proteins
  • Escherichia coli Proteins
  • PdxJ protein, E coli
  • Pyridoxal Phosphate
  • Pyridoxaminephosphate Oxidase
  • Ligases
  • pyridoxine 5-phosphate