Arguments are presented for the importance of electrostatics in enzyme catalysis. Theoretical calculations and specially designed experiments on serine proteases indicate that the protein electrostatic field stabilises the strongly polar transition intermediate and thus enhances the reaction rate. Similar theoretical conclusions have also been drawn for other enzymes. A hypothesis is outlined stating that specificity is enhanced if the interacting groups of the enzyme and its substrate in the transition state are of similar nature, i.e. if both are ionic, polar or apolar. The statement is supported by published experimental data from site-directed mutagenesis studies.
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