RidA proteins contribute to fitness of <i>S. enterica</i> and <i>E.</i> <i>coli</i> by reducing 2AA stress and moderating flux to isoleucine biosynthesis.

ABSTRACT: Defining the physiological role of a gene product relies on interpreting phenotypes caused by the lack, or alteration, of the respective gene product. Mutations in critical genes often lead to easily recognized phenotypes that can include changes in cellular growth, metabolism, structure etc. However, mutations in many important genes may fail to generate an obvious defect unless additional perturbations are caused by medium or genetic background. The latter scenario is exemplified by RidA proteins. In vitro RidA proteins deaminate numerous imine/enamines, including those generated by serine/threonine dehydratase IlvA (EC:4.3.1.19) from serine or threonine - 2-aminoacrylate (2AA) and 2-aminocrotonate (2AC), respectively. Despite this demonstrable biochemical activity, a lack of RidA

SUBMITTER: Fulton RL 

PROVIDER: S-EPMC11491847 | biostudies-literature | 2024

REPOSITORIES: biostudies-literature