Purification and characterization of phosphomannomutase/phosphoglucomutase from Pseudomonas aeruginosa involved in biosynthesis of both alginate and lipopolysaccharide

Purification and characterization of phosophomannomutase (PMM) derived from Pseudomonas aeruginosa show that the PMM enzyme affects the biosynthesis of alginate and lipopolysaccharide by using both phosphomannose and phosphoglucose as substrates. PMM catalyzes the interconversion of mannose 1-phosphate, mannose 6-phosphate, glucose 1-phosphate and glucose 6-phosphate and the conversion of ribose 1-phosphate and 2-deoxyglucose 6-phosphate. The enzymes PMM and phosphoglucomutase do not affect the nonmucoid algC mutant strain 8858 and the LPS-rough algC mutant strain AK1012.