Sucrose:(1→6)-α- D-glucan 6-α- D-glucosyltransferase Sucrose 6-glucosyltransferase SGE CEP sucrose-1,6-α-glucan glucosyltransferase sucrose:1,6-α- D-glucan 6-α- D-glucosyltransferase Synthesis of a polysaccharide of the starch-glycogen class from sucrose by a cell-free, bacterial enzyme system (amylosucrase). Enzymic synthesis and reactions of a sucrose isomer α- D-galactopyranosyl-β- D-fructofuranoside. This enzyme extends the glucan chain by an α(1→4) linkage.įeingold, D.S., Avigad, G.
In some cases, in which the enzyme forms more than one linkage type, classification relies on the relative proportion of the linkages that are generated. They are classified based on the linkage by which they attach the transferred residue. The glucansucrases transfer a D-glucosyl residue from sucrose to a glucan chain. Sucrose:(1→4)-α- D-glucan 4-α- D-glucosyltransferase Sucrose-glucan glucosyltransferase sucrose-1,4-α-glucan glucosyltransferase sucrose:1,4-α- D-glucan 4-α- D-glucosyltransferase Now included with EC 2.4.1.25, 4-α-glucanotransferase The biological synthesis of dextran from dextrins. Bacterial conversion of dextrin into a polysaccharide with the serological properties of dextran. Enzymic synthesis of polysaccharides: a biological type of polymerization. (1→4)-α- D-glucan:(1→6)-α- D-glucan 6-α- D-glucosyltransferaseīRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: n + m = n-1 + m+1ĭextrin 6-glucosyltransferase dextran dextrinase 1,4-α- D-glucan:1,6-α- D-glucan 6-α- D-glucosyltransferase (Ed.), Essays in Biochemistry, vol. 6, Academic Press, London and New York, 1970, pp. The structure, function and control of glycogen phosphorylase. Purification and properties of glycogen phosphorylase from Escherichia coli.
Lobster muscle phosphorylase: purfication and properties. A simple method for the preparation of crystalline potato phosphorylase and Q-enzyme. Preparation, properties, and molecular weight. The breakdown and synthesis of starch by an enzyme from pea seeds. maltodextrin phosphorylase, starch phosphorylase, etc.īRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: The accepted name of the enzyme should be modified for each specific instance by substituting "glycogen" with the name of the natural substrate, e.g. The enzyme stops when it reaches the fourth residue away from an α-1,6 branching point, leaving a highly branched core known as a limit dextrin. Some of these enzymes catalyse the first step in the degradation of large branched glycan polymers - the phosphorolytic cleavage of α-1,4-glucosidic bonds from the non-reducing ends of linear poly(1→4)-α- D-glucosyl chains within the polymers. This entry covers several enzymes from different sources that act in vivo on different forms of (1→4)-α- D-glucans. (1→4)-α- D-glucan:phosphate α- D-glucosyltransferase Muscle phosphorylase a and b amylophosphorylase polyphosphorylase amylopectin phosphorylase glucan phosphorylase α-glucan phosphorylase 1,4-α-glucan phosphorylase glucosan phosphorylase granulose phosphorylase maltodextrin phosphorylase muscle phosphorylase myophosphorylase potato phosphorylase starch phosphorylase 1,4-α- D-glucan:phosphate α- D-glucosyltransferase phosphorylase ( ambiguous) N + phosphate = n-1 + α- D-glucose 1-phosphate
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