Glycolytic pathway enzyme (None)

Glycolytic pathway enzymes in bacteria are essential proteins participating in the stepwise breakdown of glucose to pyruvate (glycolysis), yielding ATP and NADH—crucial for bacterial viability. This pathway includes specific enzymes such as hexokinase (glucokinase), phosphoglucose isomerase, phosphofructokinase, aldolase, triosephosphate isomerase, glyceraldehyde-3-phosphate dehydrogenase (GAPDH), phosphoglycerate kinase, phosphoglycerate mutase, enolase, and pyruvate kinase. Many are encoded by essential genes in bacteria such as Bacillus subtilis and Escherichia coli[1][2][7]. Due to both the essentiality and the conserved nature of these enzymes, they are attractive targets for novel antibacterial approaches, but targeting must avoid interference with homologous human enzymes to limit toxicity[1][7]. Key individual enzymes in bacterial glycolysis and their standard names: - Hexokinase (HK) - Phosphoglucose isomerase (PGI) - Phosphofructokinase (PFK) - Fructose-bisphosphate aldolase (ALDO) - Triosephosphate isomerase (TPI) - Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) - Phosphoglycerate kinase (PGK) - Phosphoglycerate mutase (PGM) - Enolase (ENO) - Pyruvate kinase (PK)[6][7] For structured knowledge, each enzyme should be annotated separately, not the pathway as a whole. Note: This query refers to a pathway (set of enzymes), not a single target. Each enzyme listed above is a canonical molecular target; structured data models should enumerate them individually for clarity and utility in biomedical informatics.

Other names

Glycolytic enzymesglycolysis enzymesEmbden-Meyerhof pathway enzymescentral metabolic enzymes

Inhibition of enzyme catalytic activity (competitive, allosteric, covalent mechanisms) Blockade of ATP generation or precursor metabolite biosynthesis, leading to bacteriostasis or bactericidal effects