Abstract
A metal ion in the catalytic site is needed for the function of another important class of enzymes that cleave peptide and ester bonds. By coordinating the metal ion, these enzymes activate a water molecule for nucleophilic attack on the bond that is to be cleaved. The water molecule experiences a drastic change in its pK a value in this state. By far, zinc is the most commonly used metal ion in these enzymes, but iron, cadmium, cobalt, or manganese are also found. The presence of a metal ion is essential for the activity of the protease or esterase. If the metal ion is removed from the enzyme by the addition of a strong complexation reagent, for example, β-mercaptoethanol or ethylenediaminetetraacetic acid (EDTA), the catalytic activity is not observable anymore.
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Klebe, G. (2013). Inhibitors of Hydrolyzing Metalloenzymes. In: Klebe, G. (eds) Drug Design. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-17907-5_25
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DOI: https://doi.org/10.1007/978-3-642-17907-5_25
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