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. 1996 Apr;178(8):2445–2449. doi: 10.1128/jb.178.8.2445-2449.1996

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.

T K Man 1, G Zhao 1, M E Winkler 1
PMCID: PMC177961  PMID: 8636054

Abstract

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.

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Selected References

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