Enzyme-catalyzed organic synthesis of sucrose and trehalose with in situ regeneration of UDP-glucose.
This paper describes cell-free enzymatic syntheses of sucrose and trehalose using partially-purified preparations of sucrose and trehalose synthetase. The coupling of the regeneration of uridine-5'-diphosphoglucose (UDP-Glc) with synthesis of the disaccharide offers a practical route to millimol quantities of these carbohydrates. The syntheses used pyruvate kinase, UDP-Glc pyrophosphorylase, and inorganic pyrophosphatase, and the regenerated UDP-Glc was cycled approximately 10 times.
Haynie
S L
SL
Department of Chemistry, Massachusetts Institute of Technology, Cambridge 02139.
Whitesides
G M
GM
D002384:Catalysis; D004187:Disaccharides / Q000096:biosynthesis*; D004800:Enzymes, Immobilized / Q000378:metabolism; D005964:Glucosyltransferases / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D013395:Sucrose / Q000096:biosynthesis*; D014199:Trehalose / Q000096:biosynthesis*; D014908:Triticum / Q000201:enzymology; D014532:Uridine Diphosphate Glucose / Q000378:metabolism*; D014539:Uridine Diphosphate Sugars / Q000378:metabolism*
D004187:Disaccharides; D004800:Enzymes, Immobilized; D014539:Uridine Diphosphate Sugars; D013395:Sucrose; D014199:Trehalose; D005964:Glucosyltransferases; C022699:sucrose synthase; C023180:trehalose-6-phosphate synthase; D014532:Uridine Diphosphate Glucose