ABS 049: Linking Bioinformatic Classification of Rid Proteins to Substrate Specificity and Enzymatic Activity

Jered Miller ¹

¹ University of Georgia, GA, USA

Van Wickle (2025) Volume 1, ABS 049

Introduction: The critical Rid (Reactive intermediate deaminase) superfamily of proteins, characterized as an imine/enamine deaminase, is conserved throughout all domains of life. This superfamily of proteins is divided into eight subfamilies based on bioinformatic classification of primary structure. Rid1-3 proteins have been shown to process similar catalytic function, although proteins in these subfamilies have been poorly categorized due to a relative lack of research on the subject. These proteins share a conserved Arg105 residue, which has been linked to their shared similar deaminase function and links Rid1-3 proteins and substrate specificities of these proteins. 
To date, 29 proteins representing both Rid1 and Rid2 have been purified, and resultant protein using six amino acid-derived imines chosen to be representative of the chemical properties of their side chains. Preliminary data shows correlations within and across putative subgroups of Rid proteins. Once the remaining 9 proteins are assayed, the obtained LOX assay data will be used to find correlation between bioinformatic classification, conserved motifs, and biochemical activity of Rid1-3 proteins, with the goal of allowing observation about the substrate specific differences in each subfamily of proteins to be drawn. This characterization of Rid1-3 enzymatic activity will provide a more holistic understanding of the connection between of structure and Rid protein activity, provide a starting point for future in-depth studies aimed at classifying Rid proteins of unknown subfamily, and possibly initiate or guide further investigation aimed at redefining subclassification groupings as a whole.