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

Abstract

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