Question 11 pts When chymotrypsin is assayed with the surrogate substrate p-nitrophenylacetate, a rapid burst of colored...

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Biology

Question 11 pts
When chymotrypsin is assayed with the surrogate substratep-nitrophenylacetate, a rapid burst of colored productformation (p-nitrophenolate) is observed, corresponding toa relatively steep slope on the A410 vs. time (seconds)plot, followed by a slower-but-steady release ofp-nitrophenolate, corresponding to a relatively less-steepslope on the A410vs. time (seconds) plot. These resultswere interpreted as:
a) the rapid release of the first product(p-nitrophenolate), followed by the slower reaction ofacetate ion (the other product) with a catalytic lysine residue onthe enzyme
b) the unusual properties of aromatic esters and thus notapplicable to the normal chymotrypsin mechanism, which involves thehydrolysis of peptide bonds
c) the rapid release of p-nitrophenol, followed by theslower formation of the p-nitrophenolate ion
d) the rapid release of the first product(p-nitrophenolate), followed by the slower hydrolysis ofthe acyl-enzyme intermediate

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4.2 Ratings (608 Votes)

Proteases cleave proteins by a hydrolysis reactionthe addition of a molecule of water to a peptide bondAlthough the hydrolysis of peptide bonds is thermodynamically favored such hydrolysis reactions are extremely slow Bchymotrypsin cleaves peptide bonds selectively on the carboxylterminal side of the large hydrophobic amino acids such as tryptophan See Answer

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