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Protease mechanisms

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Protease mechanisms
Polypeptides can be cleaved either chemically or enzymatically. Enzymes that catalyse the hydrolytic cleavage of peptide bonds are called proteases. Proteases fall into four main mechanistic classes: serine, cysteine, aspartyl and metalloproteases. In the active sites of serine and cysteine proteases, the eponymous residue is usually paired with a proton-withdrawing group to promote nucleophilic attack on the peptide bond. Aspartyl proteases and metalloproteases activate a water molecule to serve as the nucleophile, rather than using a functional group of the enzyme itself. However, the overall process of peptide bond scission is essentially the same for all protease classes. Soluble serine proteases (a); cysteine proteases (b); aspartyl proteases (c); and metalloproteases (d).

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How do enzymes cause tremendous increases in reaction rates? Learn how a group of enzymes called the serine proteases work.


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