2400-71-7Relevant articles and documents
The synthesis of novel chromogenic enzyme substrates for detection of bacterial glycosidases and their applications in diagnostic microbiology
Burton, Michael,Perry, John D.,Stanforth, Stephen P.,Turner, Hayley J.
, p. 4841 - 4849 (2018)
The preparation and evaluation of chromogenic substrates for detecting bacterial glycosidase enzymes is reported. These substrates are monoglycoside derivatives of the metal chelators catechol, 2,3-dihydroxynaphthalene (DHN) and 6,7-dibromo-2,3-dihydroxyn
Purification, characterization, and gene identification of an α-glucosyl transfer enzyme, a novel type α-glucosidase from Xanthomonas campestris WU-9701
Sato, Toshiyuki,Hasegawa, Nobukazu,Saito, Jun,Umezawa, Satoru,Honda, Yuki,Kino, Kuniki,Kirimura, Kohtaro
body text, p. 20 - 27 (2012/09/05)
The α-glucosyl transfer enzyme (XgtA), a novel type α-glucosidase produced by Xanthomonas campestris WU-9701, was purified from the cell-free extract and characterized. The molecular weight of XgtA is estimated to be 57 kDa by SDS-PAGE and 60 kDa by gel filtration, indicating that XgtA is a monomeric enzyme. Kinetic properties of XgtA were determined for α-glucosyl transfer and maltose-hydrolyzing activities using maltose as the α-glucosyl donor, and if necessary, hydroquinone as the acceptor. The Vmax value for α-glucosyl transfer activity was 1.3 × 10-2 (mM/s); this value was 3.9-fold as much as that for maltose-hydrolyzing activity. XgtA neither produced maltooligosaccharides nor hydrolyzed sucrose. The gene encoding XgtA that contained a 1614-bp open reading frame was cloned, identified, and highly expressed in Escherichia coli JM109 as the host. Site-directed mutagenesis identified Asp201, Glu270, and Asp331 as the catalytic sites of XgtA, indicating that XgtA belongs to the glycoside hydrolase family 13.
The Substrate Specificity of Amyloglucosidase (AMG). Part IV. Hydroxycyclohexyl Glucosides
Bock, Klaus,Refn, Susanne
, p. 373 - 380 (2007/10/02)
Cyclohexyl- and (1R,2R)- and (1S,2S)-hydroxycyclohexyl α-D-glucosides have been synthesised under halide-catalysed glycosylation reaction conditions.Furthermore, phenyl and 2-hydroxyphenyl α-D-glucopyranosides have been synthesised using fusion reactions in 60-70percent yield.Finally, methyl 4-O-(β-L-galactopyranosyl)-β-D-glucopyranoside has been prepared in high yield using silver triflate-promoted glycosylation conditions.All compounds have been characterised by NMR spectroscopy and their preferred solution conformations inferred from the NMR data and hard-sphere exo-anomeric effect calculations (HSEA).All the above-mentioned compounds have been investigated as potential substrates for the enzyme amyloglucosidase (AMG).The results show that only the compounds which have a preferred ground-state conformation similar to that of maltose can act as substrates for the enzyme.
