Studies on cyclodextrin glycosyltransferase. IV. Enzymatic synthesis of 3-O-alpha-D-glucopyranosyl-L-sorbose and 4-O-alpha-D-glucopyranosyl-D-xylose using cyclodextrin glycosyltransferase.
The acceptor specificity of the transglycosylation reaction of cyclodextrin glycosyltransferase[EC 2.4.1.19] was investigated using various sugars and sugar alcohols. L-Sorbose, D-xylose, and D-galactose, which contain configurational or structural changes relative to the D-glucopyranose unit at positions other than position 1, were also shown to be efficient acceptors in the transglycosylation reaction of this enzyme. It was shown by chemical and enzymatic methods that this enzyme could transfer glycosyl residues only to the C3-hydroxyl group of L-sorbose and C4-hydroxyl group of D-xylose, producing oligosaccharides terminated by 3-O-alpha-D-glucopyranosyl-L-sorbose and 4-O-alpha-D-glucopyranosyl-D-xylose at the reducing ends, respectively.
D000085:Acetates; D001407:Bacillus / Q000201:enzymology; D005690:Galactose; D005947:Glucose; D005964:Glucosyltransferases / Q000378:metabolism*; D007854:Lead; D009844:Oligosaccharides / Q000032:analysis / Q000096:biosynthesis*; D013013:Sorbose; D013329:Structure-Activity Relationship; D014994:Xylose
D000085:Acetates; D009844:Oligosaccharides; D007854:Lead; D014994:Xylose; D005964:Glucosyltransferases; D005947:Glucose; D013013:Sorbose; D005690:Galactose