Decreased coenzyme A levels in ridA mutant strains of Salmonella enterica result from inactivated serine hydroxymethyltransferase

Mol Microbiol. 2013 Aug;89(4):751-9. doi: 10.1111/mmi.12313. Epub 2013 Jul 19.


The RidA/Yer057/UK114 family of proteins is well represented across the domains of life and recent work has defined both an in vitro activity and an in vivo role for RidA. RidA proteins have enamine deaminase activity, and in their absence the reactive 2-aminoacrylate (2-AA) accumulates and inactivates at least some pyridoxal 5'-phosphate (PLP)-containing enzymes in Salmonella enterica. The conservation of RidA suggested that 2-AA was a ubiquitous cellular stressor that was generated in central metabolism. Phenotypically, strains of S. enterica that lack RidA accumulated significantly more pyruvate in the growth medium than wild-type strains. Here we dissected this ridA mutant phenotype and showed it was an indirect consequence of damage to serine hydroxymethyltransferase (GlyA; E.C. The results here identified a fourth PLP enzyme as a target of enamine stress in Salmonella.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Acrylates / metabolism
  • Aminohydrolases / genetics*
  • Aminohydrolases / metabolism*
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / metabolism*
  • Coenzyme A / metabolism*
  • Coenzymes / metabolism
  • Culture Media / chemistry
  • Gene Deletion
  • Glycine Hydroxymethyltransferase / genetics*
  • Glycine Hydroxymethyltransferase / metabolism*
  • Pyridoxal Phosphate / metabolism
  • Pyruvic Acid / metabolism
  • Salmonella typhimurium / enzymology*
  • Salmonella typhimurium / genetics
  • Salmonella typhimurium / metabolism*


  • Acrylates
  • Bacterial Proteins
  • Coenzymes
  • Culture Media
  • Pyridoxal Phosphate
  • Pyruvic Acid
  • Glycine Hydroxymethyltransferase
  • Aminohydrolases
  • Coenzyme A