Simultaneous purification and characterization of glucokinase, fructokinase and glucose-6-phosphate dehydrogenase from Zymomonas mobilis.
The three enzymes glucokinase (EC 2.7.1.2), fructokinase (EC 2.7.1.4) and glucose-6-phosphate dehydrogenase (EC 1.1.1.49) were isolated in high yield from extracts of Zymomonas mobilis. The principal steps in the isolation procedures involved the use of selected dye-ligand adsorbent columns, with affinity elution of two of the three enzymes. Glucokinase and fructokinase are dimeric proteins (2 X 33000 Da and 2 X 28000 Da respectively) and glucose-6-phosphate dehydrogenase is a tetramer (4 X 52000 Da). Some similarities in the structural and kinetic parameters of the two kinases were noted, but they have absolute specificity for their substrates. Fructokinase is strongly inhibited by glucose; otherwise non-substrate sugars had little effect on any of the three enzymes.
Scopes
R K
RK
Testolin
V
V
Stoter
A
A
Griffiths-Smith
K
K
Algar
E M
EM
D000327:Adsorption; D001419:Bacteria / Q000201:enzymology*; D050260:Carbohydrate Metabolism; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D005631:Fructokinases / Q000302:isolation & purification / Q000378:metabolism*; D005941:Glucokinase / Q000302:isolation & purification / Q000378:metabolism*; D005954:Glucosephosphate Dehydrogenase / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D046911:Macromolecular Substances; D010770:Phosphotransferases / Q000378:metabolism*; D013379:Substrate Specificity
D046911:Macromolecular Substances; D005954:Glucosephosphate Dehydrogenase; D010770:Phosphotransferases; D005631:Fructokinases; D005941:Glucokinase; C046173:fructokinase