Mannose phosphorylation by glucokinase from liver and transplantable insulinoma. Cooperativity and discrimination of anomers.
Glucokinase from rat liver or transplantable, radiation-induced insulinomas was partially purified by ion exchange chromatography using DEAE-Cibacron Blue F3GA agarose. Phosphorylation of alpha,beta-D-mannose by glucokinase occurred with cooperative rate dependence on mannose concentration (nH: 1.50). Half-maximal phosphorylation rate occurred at 14 mM alpha,beta-D-mannose. The alpha- and beta-anomers of mannose were phosphorylated with sigmoidal kinetics (nH: 1.57 and 1.42, respectively). The affinity of glucokinase for alpha-D-mannose is higher than for beta-D-mannose (S0.5: 12 mM versus 19 mM). The maximum phosphorylation rate is slightly higher, about 10%, with beta-D-mannose than with alpha-D-mannose. Islet glucokinase has previously been shown to be chromatographically and kinetically identical to glucokinase from insulinoma and liver; therefore, evidence that glucokinase from these two tissues phosphorylates mannose with cooperative rate dependence and differentiates mannose anomers supports the glucokinase-glucose sensor hypothesis.
D007516:Adenoma, Islet Cell / Q000201:enzymology*; D000818:Animals; D005941:Glucokinase / Q000302:isolation & purification / Q000378:metabolism*; D007340:Insulinoma / Q000201:enzymology*; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008297:Male; D008358:Mannose / Q000378:metabolism*; D009368:Neoplasm Transplantation; D010766:Phosphorylation; D051381:Rats; D011919:Rats, Inbred Strains; D013237:Stereoisomerism; D013379:Substrate Specificity
D005941:Glucokinase; D008358:Mannose