Glycogenin is an enzyme involved in converting glucose to glycogen. It acts as a primer, by polymerizing the first few glucose molecules, after which other enzymes take over. It is a homodimer of 37-kDa subunits and is classified as a glycosyltransferase.
1,4-alpha-glucan-branching enzyme, also known as brancher enzyme or glycogen-branching enzyme is an enzyme that in humans is encoded by the GBE1 gene.
In enzymology, a 1,4-alpha-glucan 6-alpha-glucosyltransferase is an enzyme that catalyzes the chemical reaction that transfers an alpha-D-glucosyl residue in a 1,4-alpha-D-glucan to the primary hydroxyl group of glucose or 1,4-alpha-D-glucan.
In enzymology, a 1,3-beta-D-glucan phosphorylase is an enzyme that catalyzes the chemical reaction
In enzymology, an alpha-1,3-glucan synthase is an enzyme that catalyzes the chemical reaction
In enzymology, an alpha-1,4-glucan-protein synthase (ADP-forming) is an enzyme that catalyzes the chemical reaction
In enzymology, an amylosucrase is an enzyme that catalyzes the chemical reaction
In enzymology, a cellodextrin phosphorylase is an enzyme that catalyzes the chemical reaction
In enzymology, a cellulose synthase (GDP-forming) is an enzyme that catalyzes the chemical reaction
In enzymology, a dextransucrase is an enzyme that catalyzes the chemical reaction
In enzymology, a 4-alpha-glucanotransferase is an enzyme that catalyzes a chemical reaction that transfers a segment of a 1,4-alpha-D-glucan to a new position in an acceptor carbohydrate, which may be glucose or a 1,4-alpha-D-glucan.
In enzymology, an alternansucrase is an enzyme that catalyzes a chemical reaction that transfers an alpha-D-glucosyl residue from sucrose alternately to the 6- and 3-positions of the non-reducing terminal residue of an alpha-D-glucan, thereby creating a glucan with alternating alpha-1,6- and alpha-1,3-bonds. The name "alternan" was coined in 1982 for the glucan based on its alternating linkage structure.
In enzymology, a cyclomaltodextrin glucanotransferase is an enzyme that catalyzes the chemical reaction of cyclizing part of a 1,4-alpha-D-glucan molecule through the formation of a 1,4-alpha-D-glucosidic bond. They are bacterial enzymes belonging to the same family of the α-amylase specifically known as glycosyl-hydrolase family 13. This peculiar enzyme is capable of catalyzing more than one reaction with the most important being the synthesis of non-reducing cyclic dextrins known as cyclodextrins starting from starch, amylose, and other polysaccharides.
In enzymology, a NDP-glucose—starch glucosyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a starch synthase is an enzyme that catalyzes the chemical reaction
In enzymology, a sucrose-1,6-alpha-glucan 3(6)-alpha-glucosyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a xyloglucan 4-glucosyltransferase is an enzyme that catalyzes the chemical reaction in which a beta-D-glucosyl residue is transferred from UDP-glucose to another glucose residue in xyloglucan, linked by a beta-1,4-D-glucosyl-D-glucose bond.
In enzymology, an oligosaccharide 4-alpha-D-glucosyltransferase is an enzyme that catalyzes the chemical reaction in which the non-reducing terminal alpha-D-glucose residue is transferred from a 1,4-alpha-D-glucan to the 4-position of an alpha-D-glucan. This enzyme is useful in hydrolyzing oligosaccharides.
α-Glucans (alpha-glucans) are polysaccharides of D-glucose monomers linked with glycosidic bonds of the alpha form. α-Glucans use cofactors in a cofactor site in order to activate a glucan phosphorylase enzyme. This enzyme causes a reaction that transfers a glucosyl portion between orthophosphate and α-I,4-glucan. The position of the cofactors to the active sites on the enzyme are critical to the overall reaction rate thus, any alteration to the cofactor site leads to the disruption of the glucan binding site.
Glucan 1,6-α-isomaltosidase is an enzyme with systematic name 6-α-D-glucan isomaltohydrolase. It catalyses hydrolysis of (1→6)-β-D-glucosidic linkages in polysaccharides, to remove successive isomaltose units from the non-reducing ends of the chains
