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Research demonstrates that phosphoglucasamine mutase gene of Pseudomonas aeruginosa complements Escherichia coli cells deficient in this gene. Results point out that the protein encoded by the gene exhibits phosphoglucosamine mutase activity.

Research demonstrates that purified phosphoglucosamine mutase from Escherichia coli phosphorylates itself in the presence of ATP. Data indicate that the amino acid residue involved in the phosphorylation is serine S102 at the active-site of the enzyme.

The Staphylococcus aureus femR315 gene's role in the interruption that results in reduced methicillin resistance was analyzed. The S. aureus strain COL. femR315 showed significant amino acid sequence homology with phosphoglucomutases and other similar enzymes catalyzing isomerization of hexoses and hexosamine phosphates. A staphylococcal femR315 gene can also fully complement a well-characterized glmM deficiency.

Microbial exopolysaccharides (EPSs) synthesized by lactic acid bacteria (LAB) play a major role in the manufacturing of fermented dairy products. EPS production is characterized by a large variety in terms of quantity, chemical composition, molecular size, charge, type of sidechains and rigidity of the molecules. Monosaccharide unit's composition, linkages, charge and size determine the EPS' intrinsic properties and their interactions with other milk constituents. EPSs contribute to texture, mouthfeel, taste perception and stability of the final product. Furthermore, it was reported that EPS from food grade organisms, particularly LAB, have potential as food additives and as functional food ingredients with both health and economic benefits. A better understanding of structure-function relationships of EPS in a dairy food matrix and of EPS biosynthesis remain two major challenges for further applications of EPS and the engineering of functional polysaccharides.