Preference of glucokinase for the alpha anomer of hexose: relation to alpha-anomer preference in hexose-induced insulin release by pancreatic islets.
The alpha anomers of glucose and mannose were more rapidly phosphorylated than the beta anomers by rat liver glucokinase, whose chromatographic and kinetic properties are known to be quite similar to those of pancreatic islet glucokinase. This result may explain our previous findings of the alpha-anomeric preference in glucose- and mannose-stimulated insulin release, and therefore suggests to support the hypothesis that glucokinase in islets functions as a crucial hexose sensing enzyme for insulin release induced by glucose and mannose.
D000818:Animals; D005941:Glucokinase / Q000378:metabolism*; D005947:Glucose / Q000494:pharmacology*; D007328:Insulin / Q000378:metabolism*; D000078790:Insulin Secretion; D007515:Islets of Langerhans / Q000187:drug effects / Q000378:metabolism*; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008358:Mannose / Q000494:pharmacology*; D051381:Rats; D011919:Rats, Inbred Strains; D013237:Stereoisomerism
D007328:Insulin; D005941:Glucokinase; D005947:Glucose; D008358:Mannose