Reactive intermediate deaminase A (RidA)

Reactive intermediate deaminase A (RidA) is an evolutionarily conserved enzyme found in bacteria, archaea, and eukaryotes. RidA belongs to the Rid (YjgF/YER057c/UK114) superfamily and catalyzes the hydrolysis (deamination) of reactive enamine and imine intermediates, such as 2-aminoacrylate, generated by pyridoxal 5'-phosphate (PLP)-dependent enzymatic reactions. These intermediates, if not rapidly detoxified, can inactivate other essential PLP-dependent enzymes, leading to metabolic damage. By converting unstable and potentially harmful intermediates to stable keto acids, RidA safeguards cellular metabolism and supports amino acid biosynthesis. In addition to its primary enzymatic role, RidA has been reported to display molecular chaperone activity during oxidative stress and may possess ribonuclease or translational inhibition functions in some homologs, especially in higher eukaryotes. RidA dysfunction or deficiency has pleiotropic cellular impacts, and variants have been linked to altered amino acid biosynthesis, stress responses, and possibly cancer progression[1][2][3][4][5].

Other names

2-iminobutanoate/2-iminopropanoate deaminaseHRSP12hp14.5p14.5UK114P14.5PSP14.5 kDa translational inhibitor proteinHeat-responsive protein 12Translation inhibitor L-PSP ribonucleaseUK114 antigen homologperchloric acid-soluble proteinreactive intermediate imine deaminase A homologribonuclease UK114translational inhibitor p14.5