PMID:1833241
| Citation |
Deville-Bonne, D, Laine, R and Garel, JR (1991) Substrate antagonism in the kinetic mechanism of E. coli phosphofructokinase-1. FEBS Lett. 290:173-6 |
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| Abstract |
In the presence of its allosteric activator GDP, the major phosphofructokinase-1 from Escherichia coli K12 follows Michaelis-Menten kinetics. The kinetic behavior observed at steady-state using different concentrations of the substrates ATP and fructose-6-phosphate and the pattern of inhibition by the substrate analogs adenylyl-(beta, gamma-methylene)-diphosphonate and D-arabinose-5-phosphate are consistent with a random sequential mechanism in rapid equilibrium, rather than with an ordered binding as was suggested earlier. However, ATP and fructose-6-phosphate do not bind independently to the same active site, since the apparent affinity for one substrate is decreased about 20-fold when the other substrate is already bound. The antagonism between ATP and fructose-6-phosphate shows that a negative interaction occurs during the reaction with E. coli phosphofructokinase-1 which must be considered in addition to its allosteric properties. |
| Links | |
| Keywords |
Adenosine Triphosphate/analogs & derivatives; Adenosine Triphosphate/metabolism; Adenosine Triphosphate/pharmacology; Allosteric Regulation; Escherichia coli/enzymology; Fructosephosphates/metabolism; Guanosine Diphosphate/metabolism; Kinetics; Pentosephosphates/pharmacology; Phosphofructokinase-1/antagonists & inhibitors; Phosphofructokinase-1/metabolism |
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