Open AccessIsolation of a pdxJ point mutation that bypasses the requirement for the PdxH oxidase in pyridoxal 5' -phosphate coenzyme biosynthesis in Escherichia coli K-12
Author(s) -
Tsz-Kwong Man,
Genshi Zhao,
Malcolm E. Winkler
Publication year - 1996
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.178.8.2445-2449.1996
Subject(s) - biology , biochemistry , cofactor , point mutation , mutant , pyridoxal , biosynthesis , pyridoxal phosphate , escherichia coli , serine , mutation , glycine , oxidase test , microbiology and biotechnology , phosphate , amino acid , enzyme , gene
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.