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

2013; Wiley; Volume: 89; Issue: 4 Linguagem: Inglês

10.1111/mmi.12313

1365-2958

Jeffrey M. Flynn, Melissa R. Christopherson, Diana M. Downs,

Metabolism and Genetic Disorders

Summary The RidA / Yer 057/ UK 114 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 S almonella 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 . 2.1.2.1). The results here identified a fourth PLP enzyme as a target of enamine stress in S almonella .