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Phosphorolysis is the cleavage of a compound in which inorganic phosphate is the attacking group. It is analogous to hydrolysis. [1]An example of this is glycogen breakdown by glycogen phosphorylase, which catalyzes attack by inorganic phosphate on the terminal glycosyl residue at the nonreducing end of a glycogen molecule.
Glycogen synthase (UDP-glucose-glycogen glucosyltransferase) is a key enzyme in glycogenesis, the conversion of glucose into glycogen. It is a glycosyltransferase ( EC 2.4.1.11 ) that catalyses the reaction of UDP-glucose and (1,4- α - D -glucosyl) n to yield UDP and (1,4- α - D -glucosyl) n+1 .
B-type chains, making half of the branches, have two branch points, and all chains have the same length. E. Meléndez-Hevia, R. Meléndez and E. I. Canela (2000) "Glycogen Structure: an Evolutionary View", pp. 319–326 in Technological and Medical Implications of Metabolic Control Analysis (ed. A. Cornish-Bowden and M. L. Cárdenas), Kluwer Academic Publishers, Dordrecht
In enzymology, a starch synthase (EC 2.4.1.21) is an enzyme that catalyzes the chemical reaction. ADP-glucose + (1,4-alpha-D-glucosyl) n ADP + (1,4-alpha-D-glucosyl) n+1 Thus, the two substrates of this enzyme are ADP-glucose and a chain of D-glucose residues joined by 1,4-alpha-glycosidic bonds, whereas its two products are ADP and an elongated chain of glucose residues.
Starch phosphorylase is a form of phosphorylase similar to glycogen phosphorylase, except that it acts upon starch instead of glycogen.. The plant alpha-glucan phosphorylase, commonly called starch phosphorylase (EC 2.4.1.1), is largely known for the phosphorolytic degradation of starch.
Glycogen phosphorylase breaks up glycogen into glucose subunits (see also figure below): (α-1,4 glycogen chain) n + Pi ⇌ (α-1,4 glycogen chain) n-1 + α-D-glucose-1-phosphate. [2] Glycogen is left with one fewer glucose molecule, and the free glucose molecule is in the form of glucose-1-phosphate.
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