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Figure 1. Enzyme-substrate complex. Note how
the pyranose ring (magenta) is distorted. This is an
excellent example of transition state stabilization and
results from the binding energy associated with binding the
R group.
Figure 2. Covalent intermediate. Note that
the pyranose ring has adopted the more stable chair
conformation. The water that is involved in hydrolysis of
the covalent intermediate is yellow.
Figure 3. Enzyme-product complex. Note that
the pyranose ring has adopted the more stable chair
conformation. In the crystal the product gives poorer
electron density than the two above structures, suggesting
that the product is poorly bound.
Biochemistry 462a http://www.biochem.arizona.edu/classes/bioc462/462a/462a.html Department of Biochemistry and Molecular Biophysics The University of Arizona mawells@email.arizona.edu All contents copyright © 1998-2000. All rights reserved. Last revision spring/summer 2000 |
