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.
Yang
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Y
Department of Microbiology and Molecular Genetics, University of Texas Houston Medical School, Houston, Texas 77030-1501, USA.
Zhao
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Man
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TK
Winkler
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ME
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