Bacterial glycolytic and related metabolic enzymes

Bacterial glycolytic and related metabolic enzymes are a group of proteins essential for the central carbon metabolism of pathogens, facilitating the conversion of glucose into energy (ATP) and biosynthetic precursors (1.2.2). Key enzymes in this category include fructose-1,6-bisphosphate aldolase (FBPA), glyceraldehyde-3-phosphate dehydrogenase (GAPDH), and pyruvate kinase, which are vital for bacterial growth and survival (1.2.1, 1.2.2). Beyond their metabolic roles, several of these enzymes function as moonlighting proteins on the bacterial surface, where they act as virulence factors by binding host proteins like plasminogen and aiding in immune evasion (1.2.2). Targeting these enzymes offers a strategy for developing novel antibiotics, particularly by exploiting structural differences between bacterial and human orthologs, such as the distinction between bacterial Class II aldolases and human Class I aldolases (1.2.1). While drugs like fosfomycin already target related metabolic steps in cell wall synthesis by mimicking phosphoenolpyruvate, research continues into specific inhibitors of the glycolytic flux to combat multi-drug resistant infections (1.3.1, 1.3.4). However, the high conservation of some metabolic pathways between bacteria and humans presents a significant challenge for achieving therapeutic selectivity and avoiding host toxicity (1.2.1, 1.3.2).

Other names

Bacterial central carbon metabolism enzymesBacterial glycolytic pathway enzymesBacterial metabolic enzymes

Inhibition of essential metabolic pathways, depletion of cellular ATP, and disruption of cell wall precursor synthesis.