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Unformatted text preview: hydrolyzes the di-amino acid Phe-Phe, there is not a burst of phenylalanine released. Why? 4. In chymotrypsin, suppose you replaced the aspartate that is part of the catalytic triad with an asparagine. How would this affect the reaction and why? serine oxygen attacks the carbonyl carbon of a peptide bond, the hydrogen-bonded His functions as a general base to abstract the serine proton, and the negatively charged Asp stabilizes the positive charge that forms on the His residue. This prevents the development of a very unstable positive charge on the serine hydroxyl and increases its nucleophilicity Asp use proton shuttle to His which enhance the Sers nicelophilicity. 5. You want to know which of two substrates that an enzyme prefers. What kinetic parameter would you compare and why? Vmax/Km defines who much a enzyme likes substrate. Specificity constant...
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