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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 1,3-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 dextrin dextranase 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.
2,4-Dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one 2-D-glucosyltransferase is an enzyme with systematic name UDP-alpha-D-glucose:2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one 2-beta-D-glucosyltransferase. This enzyme catalyses the following chemical reaction
Alpha,alpha-trehalose synthase is an enzyme with systematic name ADP-glucose:D-glucose 1-alpha-D-glucosyltransferase. This enzyme catalyses the following chemical reaction
References
- Abdullah M; Whelan WJ (1960). "Synthesis of alpha-1:6-glucosidic linkages by a transglycosylase from potato". Biochem. 75: 12P.
- Barker SA, Carrington TR (1953). "Studies of Aspergillus niger. Part II. Transglycosidation by Aspergillus niger". Journal of the Chemical Society. Lond.: 3588–3593. doi:10.1039/jr9530003588.
- Saroja K, Venkataraman R, Giri KV (July 1955). "Transglucosidation in Penicillium chrysogenum Q-176; isolation and identification of the oligosaccharides". The Biochemical Journal. 60 (3): 399–403. doi:10.1042/bj0600399. PMC 1215714 . PMID 13239572.
