Glycogen phosphorylase is one of the phosphorylase enzymes. Glycogen phosphorylase catalyzes the rate-limiting step in glycogenolysis in animals by releasing glucose-1-phosphate from the terminal alpha-1,4-glycosidic bond. Glycogen phosphorylase is also studied as a model protein regulated by both reversible phosphorylation and allosteric effects.
Glucose 1-phosphate is a glucose molecule with a phosphate group on the 1'-carbon. It can exist in either the α- or β-anomeric form.
Glycogen synthase is a key enzyme in glycogenesis, the conversion of glucose into glycogen. It is a glycosyltransferase that catalyses the reaction of UDP-glucose and n to yield UDP and n+1.
Purine nucleoside phosphorylase, PNP, PNPase or inosine phosphorylase is an enzyme that in humans is encoded by the NP gene. It catalyzes the chemical reaction
Phosphorylase kinase (PhK) is a serine/threonine-specific protein kinase which activates glycogen phosphorylase to release glucose-1-phosphate from glycogen. PhK phosphorylates glycogen phosphorylase at two serine residues, triggering a conformational shift which favors the more active glycogen phosphorylase "a" form over the less active glycogen phosphorylase b.
Myophosphorylase or glycogen phosphorylase, muscle associated (PYGM) is the muscle isoform of the enzyme glycogen phosphorylase and is encoded by the PYGM gene. This enzyme helps break down glycogen into glucose-1-phosphate, so it can be used within the muscle cell. Mutations in this gene are associated with McArdle disease, a glycogen storage disease of muscle.
Sucrose phosphorylase is an important enzyme in the metabolism of sucrose and regulation of other metabolic intermediates. Sucrose phosphorylase is in the class of hexosyltransferases. More specifically it has been placed in the retaining glycoside hydrolases family although it catalyzes a transglycosidation rather than hydrolysis. Sucrose phosphorylase catalyzes the conversion of sucrose to D-fructose and α-D-glucose-1-phosphate. It has been shown in multiple experiments that the enzyme catalyzes this conversion by a double displacement mechanism.
Glucose-1,6-bisphosphate synthase is a type of enzyme called a phosphotransferase and is involved in mammalian starch and sucrose metabolism. It catalyzes the transfer of a phosphate group from 1,3-bisphosphoglycerate to glucose-1-phosphate, yielding 3-phosphoglycerate and glucose-1,6-bisphosphate.
In enzymology, a 1,3-beta-oligoglucan phosphorylase is an enzyme that catalyzes the chemical reaction
In enzymology, an alpha,alpha-trehalose phosphorylase is an enzyme that catalyzes the chemical reaction
In enzymology, an alpha,alpha-trehalose phosphorylase (configuration-retaining) is an enzyme that catalyzes the chemical reaction
In enzymology, a cellobiose phosphorylase is an enzyme that catalyzes the chemical reaction
In enzymology, a cellodextrin phosphorylase is an enzyme that catalyzes the chemical reaction
In enzymology, a kojibiose phosphorylase is an enzyme that catalyzes the chemical reaction
In enzymology, a laminaribiose phosphorylase is an enzyme that catalyzes the chemical reaction
In enzymology, a pyrimidine-nucleoside phosphorylase is an enzyme that catalyzes the chemical reaction
In enzymology, a trehalose 6-phosphate phosphorylase is an enzyme that catalyzes the chemical reaction
In enzymology, an uridine phosphorylase is an enzyme that catalyzes the chemical reaction
In molecular biology, glycoside hydrolase family 65 is a family of glycoside hydrolases.
4-O-beta-D-mannosyl-D-glucose phosphorylase is an enzyme with systematic name 4-O-beta-D-mannopyranosyl-D-glucopyranose:phosphate alpha-D-mannosyltransferase. This enzyme catalyses the following chemical reaction
