Purification and Characterization of Azotobacter vinelandii Glucose-6-Phosphate Dehydrogenase: Dual Coenzyme Specificity

1995 ◽  
Vol 321 (1) ◽  
pp. 94-100 ◽  
Author(s):  
B.M. Anderson ◽  
C.D. Anderson
Keyword(s):  
Azotobacter Vinelandii ◽  
Purification And Characterization ◽  
Coenzyme Specificity ◽  
Glucose 6 Phosphate Dehydrogenase

scholarly journals Simultaneous purification and characterization of glucokinase, fructokinase and glucose-6-phosphate dehydrogenase from Zymomonas mobilis

1985 ◽  
Vol 228 (3) ◽  
pp. 627-634 ◽  
Author(s):  
R K Scopes ◽  
V Testolin ◽  
A Stoter ◽  
K Griffiths-Smith ◽  
E M Algar
Keyword(s):  
Kinetic Parameters ◽  
Zymomonas Mobilis ◽  
High Yield ◽  
Purification And Characterization ◽  
Glucose 6 Phosphate Dehydrogenase

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 × 33000 Da and 2 × 28000 Da respectively) and glucose-6-phosphate dehydrogenase is a tetramer (4 × 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.

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