Activation of yeast hexokinase by chelators and the enzymic slow transition due to metal-nucleotide interactions

1982 ◽  
Vol 213 (1) ◽  
pp. 14-25 ◽  
Author(s):  
Kenneth E. Neet ◽  
Thomas C. Furman ◽  
William J. Hueston
Keyword(s):  
Nucleotide Interactions ◽  
Yeast Hexokinase

scholarly journals Yeast hexokinase mutants.

1977 ◽  
Vol 252 (13) ◽  
pp. 4443-4444
Author(s):  
J M Gancedo ◽  
D Clifton ◽  
D G Fraenkel
Keyword(s):  
Yeast Hexokinase

scholarly journals Further properties and possible mechanism of action of adenosine 5′-triphosphate–d-glucose 6-phosphotransferase from rat liver

1967 ◽  
Vol 105 (2) ◽  
pp. 473-482 ◽  
Author(s):  
M. J. Parry ◽  
D G Walker
Keyword(s):  
Catalytic Properties ◽  
Gel Filtration ◽  
Thiol Group ◽  
Acceptor Molecule ◽  
Magnesium Ions ◽  
Purification Procedure ◽  
Inhibitory Effects ◽  
Bivalent Ions ◽  
Low Glucose ◽  
Yeast Hexokinase

1. Magnesium ions are the most effective bivalent ions in the glucokinase reaction. 2. The molecular weight of rat hepatic glucokinase is 48000–49000 as assessed by gel filtration on Sephadex G-100. 3. Anomalous kinetic behaviour at low glucose concentrations appears to be due to the formation during the purification procedure of fragments possessing modified catalytic properties, but is unlikely to be of physiological significance. 4. Extension of previous studies (Parry & Walker, 1966) suggests that glucokinase catalyses a reaction of the random Bi Bi type similar to that of yeast hexokinase. 5. The inhibitory effects of various thiol reagents suggest that a thiol group may be involved at or near the binding site of the acceptor molecule.

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