N-acetylglucosamine-insensitive glucose phosphorylation in isolated hepatocytes from rats fasted for 48 h.
Glucose phosphorylation in isolated hepatocytes was studied by the release of 3H from D-[2-3H]glucose. Glucokinase activity was decreased by fasting rats for 48 h and was further reduced in cells by adding 30 mM GlcNAc, a potent competitive inhibitor. Although this treatment resulted in the loss of more than 97% of glucokinase activity in hepatocytes, glucose phosphorylation proceeded at an appreciable rate. These observations demonstrate the involvement of a high -K0.5 enzyme system in addition to glucokinase in hepatocyte glucose phosphorylation.
D000117:Acetylglucosamine / Q000494:pharmacology*; D000818:Animals; D001667:Binding, Competitive; D005215:Fasting; D005941:Glucokinase / Q000378:metabolism; D005944:Glucosamine / Q000031:analogs & derivatives*; D005947:Glucose / Q000378:metabolism*; D008099:Liver / Q000187:drug effects* / Q000378:metabolism; D010766:Phosphorylation; D051381:Rats; D013997:Time Factors
D005941:Glucokinase; D005947:Glucose; D005944:Glucosamine; D000117:Acetylglucosamine