Deviations from michaelis-menten behaviour of plant glutamate dehydrogenase with ammonium as variable substrate
Abstract
A stopped flow kinetic analysis has been performed with a homogeneous protein fraction of plant glutamate dehydrogenase. The enzyme exerts strong negative cooperativity with ammonium as variable substrate. The limiting initial rate constants for low substrate concentrations, as calculated from the kinetic data, indicate that the catalytic efficiency of the enzyme increases at low ammonium concentrations. From this it becomes evident that the...
Paper Details
Title
Deviations from michaelis-menten behaviour of plant glutamate dehydrogenase with ammonium as variable substrate
Published Date
Jan 1, 1980
Journal
Volume
19
Issue
1
Pages
11 - 13
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