Phosphoglucosamine mutase (GlmM) catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate, a critical step in the biosynthesis of peptidoglycan and lipid A moieties in bacterial cell walls . In Bartonella quintana, this enzyme is likely essential for maintaining structural integrity and pathogenicity, as observed in E. coli and other gram-negative bacteria .
Peptidoglycan Synthesis: Required for polymerizing UDP-N-acetylglucosamine, a precursor for cell wall assembly .
Lipid A Biosynthesis: Supports lipopolysaccharide (LPS) production, which is vital for B. quintana survival in human hosts .
Autophosphorylation: In E. coli, GlmM requires phosphorylation via ATP for activity, with Serine 102 as the critical residue . This post-translational modification may be conserved in B. quintana, though experimental validation is lacking.
Enzyme Kinetics:
KEGG: bqu:BQ11740
STRING: 283165.BQ11740