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Decreased coenzyme A levels in ridA mutant strains of S almonella enterica result from inactivated serine hydroxymethyltransferase
Author(s) -
Flynn Jeffrey M.,
Christopherson Melissa R.,
Downs Diana M.
Publication year - 2013
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.12313
Subject(s) - biology , mutant , serine , biochemistry , enzyme , serine hydroxymethyltransferase , pyridoxal , proteases , wild type , strain (injury) , microbiology and biotechnology , gene , anatomy
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 .