3554-90-3Relevant articles and documents
Two-Step Chemoenzymatic Detection of N-Acetylneuraminic Acid-α(2-3)-Galactose Glycans
Wen, Liuqing,Zheng, Yuan,Jiang, Kuan,Zhang, Mingzhen,Kondengaden, Shukkoor Muhammed,Li, Shanshan,Huang, Kenneth,Li, Jing,Song, Jing,Wang, Peng George
supporting information, p. 11473 - 11476 (2016/10/07)
Sialic acids are typically linked α(2-3) or α(2-6) to the galactose that located at the non-reducing terminal end of glycans, playing important but distinct roles in a variety of biological and pathological processes. However, details about their respective roles are still largely unknown due to the lack of an effective analytical technique. Herein, a two-step chemoenzymatic approach for the rapid and sensitive detection of N-acetylneuraminic acid-α(2-3)-galactose glycans is described.
Regioselectivity in β-galactosidase-catalyzed transglycosylation for the enzymatic assembly of D-galactosyl-D-mannose
Miyasato, Mariko,Ajisaka, Katsumi
, p. 2086 - 2090 (2007/10/03)
The regioselectivity of β-galactosidase derived from Bacillus circulans ATCC 31382 (β-1,3-galactosidase) in transgalactosylation reactions using D-mannose as an acceptor was investigated. This D-mannose associated regioselectivity was found to be different from reactions using either GlcNAc or GalNAc as acceptors, not only for β-1,3-galactosidase but also for β-galactosidases of different origins. The relative hydrolysis rate of Galβ-pNP and D-galactosyl-D-mannoses, of various linkages, was also measured in the presence of β-1,3-galactosidase and was found to correlate well with the ratio of disaccharides formed by transglycosylation. The unexpected regioselectivity using D-mannose can therefore be explained by an anomalous specificity in the hydrolysis reaction. By utilizing the identified characteristics of both regioselectivity and hydrolysis specificity using D-mannose, an efficient method for enzymatic synthesis of β-1,3-, β-1,4- and β-1,6-linked D-galactosyl-D-mannose was subsequently established.
