Nicole L.
asked • 07/07/20Where are the cleavage sites by trypsin, chymotrypsin, and CNBr
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1 Expert Answer
Erika D. answered • 07/07/20
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The amino acid providing the carboxyl group of the bond to be cleaved sits in a pocket below the catalytic site.
In trypsin, which catalyses the hydrolysis of the esters of basic amino acids, the base of this pocket contains an acidic amino acid, aspartate, so providing a negative charge to attract in a basic amino acid side chain.
In chymotrypsin, which catalyses the hydrolysis of the esters of aromatic amino aids, the pocket is lined with small neutral amino acids, leaving room for a bulky aromatic side chain to enter.
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Connie R.
Hi Nicole, Trypsin cleaves the protein to peptides at the C terminal of lysine (K) and arginine (R) amino acids Chymotrypsin cleaves the protein to peptides at the C terminal of phenylalanine (F), tyrosine (Y), and tryptophan (W). CNBr is a chemical agent that cleaves at methionine (M). Trypsin and chymotrypsin are proteolytic enzymes while CNBr or cynogen bromide is a chemical agent. All of them are responsible for breaking down proteins into peptides. Hope this info helps.01/31/24