80446-81-7Relevant articles and documents
The action of germinated barley alpha-amylases on linear maltodextrins
MacGregor, Alex. W.,Morgan, Joan E.,MacGregor, E. Ann
, p. 301 - 314 (1992)
The actions of barley alpha-amylase isozymes 1 and 2 (EC 3.2.1.1) on malto-oligosaccharides and their p-nitrophenyl glycosides were similar, but not identical.For each isozyme, transglycosylation occurred with small substrates that were hydrolysed with difficulty, whereas the rates of hydrolysis increased with increase in the size of the substrate for both the malto-oligosaccharides and the p-nitrophenyl glycosides.A p-nitrophenyl group was found to mimic a glucose residue to a large extent.The differences in action of the isozymes are believed to be caused by differences at more than one subsite of the active site.Alysine-arginine substitution is postulated to account for some of the observed variations.
Acceptor-induced modification of regioselectivity in CGTase-catalyzed glycosylations of p-nitrophenyl-glucopyranosides
Strompen, Simon,Miranda-Molina, Alfonso,López-Munguía, Agustín,Castillo, Edmundo,Saab-Rincón, Gloria
, p. 46 - 54 (2015/03/05)
Cyclodextrin glycosyltransferases (CGTase) are reported to selectively catalyze α(1→4)-glycosyl transfer reactions besides showing low hydrolytic activity. Here, the effect of the anomeric configuration of the glycosyl acceptor on the regioselectivity of
Creation of an α-mannosynthase from a broad glycosidase scaffold
Yamamoto, Keisuke,Davis, Benjamin G.
, p. 7449 - 7453 (2012/09/21)
α-Mannosides made easy: Mutation of a family-GH31 α-glucosidase that displays plasticity to alterations at the 2-OH position of donor substrates created an efficient α-mannoside-synthesizing biocatalyst. A simple fluoride donor reagent was used for the synthesis of a range of mono-α-mannosylated conjugates using the α-mannosynthase displaying low (unwanted) oligomerization activity. Copyright