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A catalytic triad commonly refers to the three amino acid residues found inside the active site of certain protease enzymes: serine (S), aspartate (D) and histidine (H). They work together to break peptide bonds on polypeptides. More generally, catalytic triad can refer to any set of three residues that function together and are directly involved in catalysis. Because enzymes fold into complex three-dimensional shapes, the residues of a catalytic triad can be far from each other in the primary structure however are brought close together in the tertiary structure.
Additional recommended knowledge
An example of a catalytic triad is present in chymotrypsin, where the triad (on the enzyme) consists of S195 (that is the serine found at residue 195 in the protein sequence), D102 and H57. Essentially, S195 binds to the substrate polypeptide to the side of a phenylalanine, tryptophan or tyrosine residue closer to the C-terminus, holding it in place. D102 and H57 then hydrolyze the bond. This takes place in several steps.
|This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Catalytic_triad". A list of authors is available in Wikipedia.|