AnmK belongs to the peptidoglycan recycling pathway, which salvages up to 60% of cell wall components in bacteria like Escherichia coli . In Gloeobacter violaceus, AnmK phosphorylates anhMurNAc, enabling its conversion to N-acetylglucosamine-phosphate (GlcNAc-P) via subsequent enzymatic steps. This process ensures the reuse of cell wall sugars, minimizing energy expenditure on de novo synthesis .
Substrate: 1,6-anhydro-N-acetylmuramic acid (anhMurNAc)
Product: N-acetylmuramic acid-6-phosphate (MurNAc-P)
Genomic Localization: The anmK gene in Gloeobacter violaceus (UniProt Q7NEY1) is part of a conserved operon linked to cell wall recycling .
Phylogenetic Significance: Gloeobacter represents an early-branching cyanobacterium lacking thylakoid membranes, making its enzymes valuable for studying ancestral metabolic pathways .
Antibiotic Susceptibility Studies: Disruption of anmK in P. aeruginosa increases sensitivity to β-lactams like imipenem, highlighting its role in cell wall integrity .
Enzyme Engineering: Recombinant AnmK enables high-sensitivity detection of peptidoglycan fragments via radioactive labeling .
Evolutionary Biology: Comparative studies with Gloeobacter AnmK shed light on the adaptation of peptidoglycan recycling in early-diverging bacteria .
KEGG: gvi:glr3746
STRING: 251221.glr3746