Involvement of the gapA- and epd (gapB)-encoded dehydrogenases in pyridoxal 5'-phosphate coenzyme biosynthesis in Escherichia coli K-12

J Bacteriol. 1998 Aug;180(16):4294-9. doi: 10.1128/JB.180.16.4294-4299.1998.


We show that epd (gapB) mutants lacking an erythrose 4-phosphate (E4P) dehydrogenase are impaired for growth on some media and contain less pyridoxal 5'-phosphate (PLP) and pyridoxamine 5'-phosphate (PMP) than their epd+ parent. In contrast to a previous report, we found that gapA epd double mutants lacking the glyceraldehyde 3-phosphate and E4P dehydrogenases are auxotrophic for pyridoxine. These results implicate the GapA and Epd dehydrogenases in de novo PLP and PMP coenzyme biosynthesis.

Publication types

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

MeSH terms

  • Aldehyde Oxidoreductases / genetics
  • Aldehyde Oxidoreductases / metabolism
  • Escherichia coli / enzymology
  • Escherichia coli / genetics
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins*
  • Mutation / genetics
  • Oxidoreductases / genetics
  • Oxidoreductases / metabolism*
  • Pyridoxal Phosphate / biosynthesis
  • Pyridoxal Phosphate / metabolism*


  • Escherichia coli Proteins
  • Pyridoxal Phosphate
  • Oxidoreductases
  • Aldehyde Oxidoreductases
  • erythrose 4-phosphate dehydrogenase, E coli