Mannose phosphorylation by glucokinase from liver and transplantable insulinoma. Cooperativity and discrimination of anomers.

Abstract:

: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.

journal_name

Diabetes

journal_title

Diabetes

authors

Meglasson MD,Schinco M,Matschinsky FM

doi

10.2337/diab.32.12.1146

subject

Has Abstract

pub_date

1983-12-01 00:00:00

pages

1146-51

issue

12

eissn

0012-1797

issn

1939-327X

journal_volume

32

pub_type

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