MBB222-lecture10

MBB222-lecture10 - Serine Proteases Serine Proteases...

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erine Proteases Serine Proteases • enzymes that hydrolyse peptide bonds using an active-site serine • e.g., chymotrypsin, trypsin • contain a “catalytic triad” that includes the catalytically active rine serine • despite mechanistic similarities, have different substrate specificities (i.e., cleave peptide chains at different amino acid residues) • all hydrolyse peptide bonds (i.e., are proteases ) o not all share the same structure do not all share the same structure
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hymotrypsin: Chymotrypsin: • specific for peptide bonds adjacent to aromatic amino acid sidues, cleaving on the carboxyl side of the residue residues, cleaving on the carboxyl side of the residue • enhances rate of peptide bond hydrolysis by a factor of at least 10 9 • e.g., below is the N-terminus of a longer polypeptide – arrow indicates cleavage point using chymotrypsin
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• can also cleave ester linkage in the chromogenic substrate analog p-nitrophenylacetate (colourless) roduces p itrophenol produces p-nitrophenol (yellow)
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This note was uploaded on 12/13/2011 for the course MBB 201 taught by Professor -- during the Spring '11 term at Simon Fraser.

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MBB222-lecture10 - Serine Proteases Serine Proteases...

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