Glucokinase, an enzyme that catalyzes the phosphorylation of glucose, constitutes the key regulatory step in glucose metabolism in pancreatic islets and liver. We found that 3-O-methyl-N-acetyl-D-glucosamine (3-O-methyl-GlcNAc) potently inhibits glucose phosphorylation by N-acetylglucosamine kinase whereas glucokinase is not at all
The Journal of biological chemistry, 256(5), 2367-2370 (1981-03-10)
Equilibrium dialysis studies on the binding of the Dolichos biflorus lectin with [14C]methyl alpha-D-GalNAc showed that the lectin has two combining sites/molecule and an intrinsic association constant at 3 degrees C of 4.2 X 10(3) liters mol-1. Binding studies on
European journal of biochemistry, 204(3), 1165-1168 (1992-03-15)
During the search for inhibitors of N-acetylneuraminic acid biosynthesis, it was shown that 3-O-methyl-N-acetylglucosamine competitively inhibits the N-acetylglucosamine kinase of rat liver in vitro with a Ki value of 17 microM. N-Acetylmannosamine kinase is inhibited non-competitively with a Ki value
The Journal of biological chemistry, 264(2), 1027-1035 (1989-01-15)
Alkaline borohydride treatment of the cellulosome of Clostridium thermocellum yielded two major oligosaccharide-alditols, namely D-Galp-beta(1----4)-D-GalOH and (formula; see text) The compounds, isolated via gel permeation chromatography and high performance liquid chromatography, were analyzed by monosaccharide analysis, methylation analysis, gas-liquid chromatography/mass
Gas--liquid chromatography and mass spectrometry of methylated and acetylated methyl glycosides. Application to the structural analysis of glycoprotein glycans.
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