34627-06-0Relevant articles and documents
CATALYTIC VERSATILITY OF TREHALASE: SYNTHESIS OF α-D-GLUCOPYRANOSYL α-D-XYLOPYRANOSIDE FROM β-D-GLUCOSYL FLUORIDE AND α-d-XYLOSE
Kasumi, Takafumi,Brewer, Curtis F.,Reese, Elwyn T.,Hehre, Edward J.
, p. 39 - 50 (1986)
Trehalase was previously shown (see. ref. 5) to hydrolyze α-D-glucosyl fluoride, forming β-D-glucose, and to synthesize α,α-trehalose from β-D-glucosyl fluoride plus α-D-glucose.Present observations further define the enzyme's separate cosubstrate requirements in utilizing these nonglycosidic substrates. α-D-Glucopyranose and α-D-xylopyranose were found to be uniquely effective in enabling Trichoderma reesei trehalase to catalyze reactions with β-D-glucosyl fluoride.As little as 0.2mM added α-D-glucose (0.4mM α-D-xylose) substantially increased the rate of enzymically catalyzed release of fluoride from 25mM β-D-glucosyl fluoride at 0 deg C.Digests of β-D-glucosyl fluoride plus α-D-xylose yielded the α,α-trehalose analog, α-D-glucopyranosyl α-D-xylopyranoside, as a transient (ie., subsequently hydrolyzed) transfer-product.The need for an aldopyranose acceptor having an axial 1-OH group when β-D-glucosyl fluoride is the donor, and for water when α-D-glucosyl fluoride is the substrate, indicates that the catalytic groups of trehalose have the flexibility to catalyse different stereochemical reactions.
Anomeric Selectivity of Trehalose Transferase with Rare l -Sugars
Bento, Isabel,Hagedoorn, Peter-Leon,Hanefeld, Ulf,Jeffries, Cy M.,Laustsen, Jesper U.,Marsden, Stefan R.,Mestrom, Luuk,Svergun, Dmitri I.,Van Der Eijk, Hessel
, p. 8835 - 8839 (2020/09/18)
Retaining LeLoir glycosyltransferases catalyze the formation of glycosidic bonds between nucleotide sugar donors and carbohydrate acceptors. The anomeric selectivity of trehalose transferase from Thermoproteus uzoniensis was investigated for both d- and l-glycopyranose acceptors. The enzyme couples a wide range of carbohydrates, yielding trehalose analogues with conversion and enantioselectivity of >98%. The anomeric selectivity inverts from α,α-(1 → 1)-glycosidic bonds for d-glycopyranose acceptors to α,β-(1 → 1)-glycosidic bonds for l-glycopyranose acceptors, while (S)-selectivity was retained for both types of sugar acceptors. Comparison of protein crystal structures of trehalose transferase in complex with α,α-trehalose and an unnatural α,β-trehalose analogue highlighted the mechanistic rationale for the observed inversion of anomeric selectivity.
Formation of 1,1-α, α-glycosidic bonds by intramolecular aglycone delivery. A convergent synthesis of trehalose
Pratt, Matthew R.,Leigh, Clifton D.,Bertozzi, Carolyn R.
, p. 3185 - 3188 (2007/10/03)
(Matrix presented) We report a new synthesis of trehalose analogs that involves the use of intramolecular aglycone delivery for stereoselective formation of the 1,1-α,α-glycosidic bond. The glycosylation reaction afforded the desired isomer exclusively and in good yield.
Synthesis and glycosylation shift of 1,1'-disaccharides
Nishizawa,Kodama,Yamane,Kayano,Hatakeyama,Yamada
, p. 982 - 984 (2007/10/02)
Nineteen kinds of nonreducing 1,1'-disaccharides have synthesized by modified Koenigs-Knorr method, and characterized by NMR. The glycosylation shift of each anomeric carbon has been estimated.
