Bacterial glycolytic pathway enzymes

Bacterial glycolytic pathway enzymes are a collective group of proteins that mediate the stepwise catabolism of glucose into pyruvate through the Embden-Meyerhof-Parnas (EMP) pathway. These enzymes, including hexokinase, phosphofructokinase, glyceraldehyde-3-phosphate dehydrogenase (GAPDH), and enolase, are fundamental to bacterial bioenergetics, providing essential ATP and metabolic precursors for biosynthesis. Many of these enzymes are classified as essential for bacterial survival, making them attractive targets for the development of novel antimicrobial agents to combat multidrug-resistant pathogens. Beyond their primary metabolic roles, several of these proteins exhibit "moonlighting" functions, where they are translocated to the bacterial surface to act as virulence factors by binding host components like plasminogen or the extracellular matrix. Although the glycolytic pathway is highly conserved, therapeutic strategies aim to exploit structural differences between bacterial and human isoforms, such as the distinct classes of fructose-1,6-bisphosphate aldolase, to ensure selective toxicity.

Other names

Bacterial glycolytic enzymesGlycolysis enzymesEmbden-Meyerhof-Parnas pathway enzymesEMP enzymes

Enzyme inhibition