Fig. 3: Investigation of substrate specificity determinants.
From: Metformin hydrolase is a recently evolved nickel-dependent heteromeric ureohydrolase
A Overlay of the active sites of the AnMefH crystal structure (gray) and an AlphaFold model of DmgH (green). The side chains of the metal binding residues of AnMefH are shown (gray). These amino acids are identical in DmgH and MefH. Residues that were exchanged in DmgH for the corresponding residues of MefH are highlighted in blue, if substrate specificity was not changed, or red, if substrate specificity was changed. B Specific activities for the combinations of DmgH and AnMefH subunits and different variants of DmgH with 2 mM dimethylguanidine or metformin. Data represent the average ± s.d. of triplicates and consistent results were obtained with independent preparations (n = 3, error, s.d.). n.d. not detected. Source data are provided as a Source Data file.
