Regulatory Properties of the ADP-Glucose Pyrophosphorylase from the Clostridial Firmicutes Member Ruminococcus albus

The enzymes involved in glycogen synthesis fromFirmicutes have been less characterized in comparison with other bacterial groups. We performed kinetic and regulatory characterization of the ADP-glucose pyrophosphorylase fromRuminococcus albus . Our results showed that this protein that belongs to different groups fromFirmicutes (Bacillales ,Lactobacillales , andClostridiales ) presents dissimilar features. This study contributes to the understanding of how this critical enzyme for glycogen biosynthesis is regulated in theFirmicutes group, whereby we propose that these heterotetrameric enzymes, with the exception ofBacillales , are allosterically regulated. Our results provide a better understanding of the evolutionary relationship of this enzyme family inFirmicutes .