In this article, the authors compared two glycosyl transferases potentially associated with glycogen metabolism in bacteria. Both enzymes were capable of extending an α-1,4-glucan, which is their expected primary function. However, upon closer examination, it was found that they have different specificities: one enzyme (RjoGlgAc) efficiently synthesizes maltose-1P, while the other (RjoGlgAb) prefers short-chain glucans. These results suggest that the duplication of the glgA gene led to the evolution of two specialized enzymes for the production of different intracellular polysaccharides (glycogen and MGLP) in Rhodococcus jostii. Additionally, the ability of RjoGlgAc to utilize various sugar-1P molecules suggests that it could be used as a new biocatalyst for creating novel glycans using cell-free glycobiology strategies, which aligns with current
Molecular Enzymology Lab projects.
