Bacterial phosphoenolpyruvate-dependent phosphotransferase system and β-fructofuranosidase (No widely accepted single abbreviation for the combined target; individually, “PTS” for phosphotransferase system and “β-FFase” or “INV” for β-fructofuranosidase are common[1][3][4][5][6].)

The bacterial phosphoenolpyruvate-dependent phosphotransferase system (PTS) is a multi-component system responsible for active uptake and concomitant phosphorylation of various carbohydrates in bacteria, using phosphoenolpyruvate (PEP) as the phosphoryl donor. Core PTS proteins (Enzyme I, HPr, and Enzyme II complexes) mediate transport and phosphorylation of sugars such as glucose, fructose, and mannose, with membrane-spanning and cytoplasmic components[1][3][5][9]. The PTS is central to metabolic regulation and is involved in diverse cellular processes including biofilm formation, regulation of carbohydrate metabolism, chemotaxis, and bacterial virulence[1][3][5]. β-fructofuranosidase (invertase) is an enzyme of the glycoside hydrolase family 32 (GH32) that hydrolyzes the glycosidic bond in sucrose to produce glucose and fructose, as well as cleaving β-fructofuranoside residues from other oligosaccharides and fructans[2][4][6]. This enzyme is secreted by bacteria and fungi, contributing to carbohydrate metabolism. In some beneficial bacteria (e.g., Bifidobacterium species), it enables the utilization of dietary fructooligosaccharides and is important in prebiotic effects[4][6]. In food biotechnology, β-fructofuranosidases are used for the production of high-fructose syrups and prebiotic oligosaccharides, and they are being explored as biosensors[2][4]. Note: The query merges two distinct entities (the bacterial phosphotransferase system and β-fructofuranosidase), each with separate structures and biological roles, rather than a single canonical target.

Other names

PTSsugar PTSbacterial PEP:carbohydrate phosphotransferase systemInvertaseβ-FFasesucrase

PTS inhibitors block sugar uptake and metabolism, which can starve bacteria or disrupt their virulence and regulatory networks. β-fructofuranosidase inhibitors prevent hydrolysis of sucrose/fructooligosaccharides, affecting energy/metabolite acquisition in microbes.