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Enzymes perform the executive role in growth, energy conversion,
and repair of a living organism. Their activity is adjusted to
their en vironment within the cell, being turned off, switched on,
or finely tuned by specific metabolites according to demands at the
physiologi cal level. Each enzyme discovered in the long history of
enzymology has revealed its own individuality. Even closely related
members of a family differ in specificity, stability or regulatory
properties. Despite these, at first sight overwhelming aspects of
individuality, common factors of enzymic reactions have been
recognized. Enzymes are stereospecific catalysts even when a
nonspecific process would yield the same product. Knowledge of the
detailed stereochemistry of an enzymic reaction helps to deduce
reaction mechanisms and to ob tain insight into the specific
binding of substrates at the active site. This binding close to
catalytically competent groups is related to the enormous speed of
enzyme-catalyzed reactions. The physical ba sis of rate-enhancement
is understood in principle and further exploit ed in the design of
small organic receptor molecules as model enzymes. These aspects of
enzyme catalysis are discussed in Session 1. Session 2 emphasizes
the dynamic aspects of enzyme substrate inter action. Substrate
must diffuse from solution space to the enzyme's surface. This
process is influenced and can be greatly facilitated by certain
electrostatic propterties of enzymes. The dynamic events during
catalysis are studied by relaxation kinetics or NMR techniques."
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