Involvement of the gapA- and epd (gapB)-encoded dehydrogenases in pyridoxal 5'-phosphate coenzyme biosynthesis in Escherichia coli K-12.
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.
Department of Microbiology and Molecular Genetics, University of Texas Houston Medical School, Houston, Texas 77030-1501, USA.
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Yang
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Zhao
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Winkler
D000445:Aldehyde Oxidoreductases / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins; D009154:Mutation / Q000235:genetics; D010088:Oxidoreductases / Q000235:genetics / Q000378:metabolism*; D011732:Pyridoxal Phosphate / Q000096:biosynthesis / Q000378:metabolism*
D029968:Escherichia coli Proteins; D011732:Pyridoxal Phosphate; D010088:Oxidoreductases; D000445:Aldehyde Oxidoreductases; C066236:erythrose 4-phosphate dehydrogenase, E coli