User:Ann Taylor/Sandbox Trypsin
The Mechanism of TrypsinThe Mechanism of Trypsin
One of the ways we know about the mechanism of enzymes is through the use of xray crystallography structures of trapped intermediates or inhibitors bound to enzymes. In a paper by Radisky and Koshland[1], an acyl intermediate of trypsin (PDB code 2AGG was characterized. Serine proteases use a covalent mechanism to catalyze the hydrolysis of a peptide bond. A covalent bond is formed between and a substrate . The between one of the Ser O configurations and the alpha carbon of the substrate lysine is the distance of a C-O bond, indicating that the covalent intermediate is indeed formed. There is a situated in the active site, primed to cleave the acyl intermediate by the same that participates in the catalytic triad. Specificity of the proteases is determined by a binding pocket. Trypsin is specific for large, basic amino acids; its binding pocket contains an residue at the base of the pocket.
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