α-Glucosidase is in the glycoside hydrolase family 13 (13AG) and 31 (31AG). Only 31AGs can hydrate the D-glucal double bond to form α-2-deoxyglucose. Because 1,5-anhydrofructose (AF), having a 2-OH group, mimics the oxocarbenium ion transition state, AF may be a substrate for α-glucosidases. α-Glucosidase-catalyzed hydration produced α-glucose from AF, which plateaued with time. Combined reaction with α-1,4-glucan lyase and 13AG eliminated the plateau. Aspergillus niger α-glucosidase (31AG), which is stable in organic solvent, produced ethylα-glucoside from AF in 80% ethanol. The findings indicate that α-glucosidases catalyze trans-addition. This is the first report of α-glucosidase-associated glucose formation from AF, possibly contributing to the salvage pathway of unutilized AF. © 2012 by The American Society for Biochemistry and Molecular Biology, Inc.
CITATION STYLE
Kim, Y. M., Saburi, W., Yu, S., Nakai, H., Maneesan, J., Kang, M. S., … Kimura, A. (2012). A novel metabolic pathway for glucose production mediated by α-glucosidase-catalyzed conversion of 1,5-anhydrofructose. Journal of Biological Chemistry, 287(27), 22441–22444. https://doi.org/10.1074/jbc.C112.360909
Mendeley helps you to discover research relevant for your work.