Kinetic consequences of a slow substrate binding step in group transferases. Interpretation of product inhibition experiments.

  • A Himoe
  • Published 1976 in Biochimica et biophysica acta

Abstract

The steady state kinetic properties of a simple model for an enzyme catalyzed group transfer reaction between two substrates have been calculated. One substrate is assumed to bind slowly and the other rapidly to the enzyme. Apparent substrate inhibition or substrate activation by the rapidly binding substrate may result if the slowly binding substrate binds… (More)

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