Cellodextrin phosphorylase (CDP) (CDP)

Cellodextrin phosphorylase (CDP) is an enzyme belonging to the glycoside hydrolase family 94 (GH94) primarily found in cellulolytic anaerobic bacteria such as Ruminiclostridium thermocellum and Ruminococcus albus (Wikipedia; PMID: 21344678). It catalyzes the reversible phosphorolysis of beta-1,4-linked glucooligosaccharides, known as cellodextrins, into alpha-D-glucose 1-phosphate and a shortened cellodextrin acceptor (EC 2.4.1.49). This metabolic pathway is more energy-efficient for the host bacteria than simple hydrolysis because it conserves the energy of the glycosidic bond through phosphorylation, bypassing the need for an additional ATP molecule during the initial steps of glycolysis (PMID: 5773308). Although CDP is not currently utilized as a target for pharmaceutical drug development in human medicine, it is a critical biocatalyst in biotechnology for the production of functional cello-oligosaccharides, prebiotic fibers, and bioethanol (PMID: 31215119). In clinical and physiological research, its importance is mostly centered on its role within the human gut microbiome and its potential for synthesizing specialized glyco-materials for drug delivery applications (PMID: 29505763).

Other names

Beta-1,4-oligoglucan:orthophosphate glucosyltransferase1,4-beta-D-oligo-D-glucan:phosphate alpha-D-glucosyltransferaseCellodextrin-cleaving phosphorylase

The enzyme catalyzes the reversible phosphorolysis of cellodextrins by using inorganic phosphate to cleave the beta-1,4-glycosidic bond at the non-reducing end, yielding alpha-D-glucose 1-phosphate and a shortened cellodextrin.