Fig. 4: Bioinformatic and functional analyzes of MetCaCb-like paired arginase family proteins.
From: Discovery of a Ni2+-dependent heterohexameric metformin hydrolase
a Phylogenetic tree of MetCaCb-like arginase family protein pairs. The six conserved metal ion coordinating residues for each sequence are shown on the right side, and their positions in MetCa are indicated on the top of the columns. The residues with a cyan background are mutated residues, differing from the conserved residues marked with a pink background. Human arginase I (hARGI) was used as an outgroup. b MetCaCb-like protein pairs formed hexamers. The method for co-purification of AcMetCaCb, HmMetCaCb, and RsMetCaCb was similar to that for MetCaCb. Notably, elution peaks at a volume of ~12.9 mL, indicative of hexameric protein complexs, were selected for subsequent enzymatic activity tests. Purification of HmMetCaCb was accompanied by an inactive peak (15.9 mL) which corresponded to the HmMetCa monomer. c Assessment of the metformin hydrolase activity of the MetCaCb-like protein pairs. The data represent the mean values of two replicates using independent enzyme preparation. Source data are provided as a Source Data file.
