Hans-Dieter Höltje

Structure-activity studies of enzyme substrates using model interaction calculations☆

Abstract The hydrolysis rates in a series of substituted N-acetylaminoacid methylesters with acylase I depend apparently on the binding strengths of the side chains to the enzyme surface. Using a truncated model of a possible enzyme binding site we calculate the binding energies for a series of straight chain substituents. Our calculations reveal a very good correlation between the calculated energies and the hydrolysis rates, indicating the value of our receptor model. We feel this to be another example of the validity of our receptor mapping using model interaction energy calculations based on the monopoles-bond polarizabilities method.

Theoretische Untersuchungen zu Struktur-Wirkungsbeziehungen bei Monoaminoxidase-Hemmern der Cyclopropylamin-Reihe

Mit Hilfe der Monopol‐Bondpolarizability‐Methode berechnete Bindungsstärken zu einem Rezeptormodell werden benutzt, um die unterschiedlichen Hemmwirkungen auf Monoaminoxidase in einer Serie von Cyclopropylaminen zu erklären.