A recent discovery has suggested that a gene mutation results in several amino acid substitutions within an active site.The following substitutions have been identified and are each expected to form the active site: It was also noticed that a coenzyme molecule containing a hydroxyl (-OH)group binds to the mutated protein in approximately the same location as the original serine but does not alter the structure of the protein in anyway.Based on your knowledge of amino acids, enzymes, and catalysis, which of the following is a REASONABLE conclusion?
A)The mutant protein cleaves on the carboxy side of phenylalanine.
B)The mutant protein cleaves peptide bonds on the carboxy side of glutamate or aspartate.
C)The mutant protein cleaves peptide bonds on the carboxy side of lysine or arginine.
D)The mutant protein functions identical to chymotrypsin.
E)The mutant protein has no function.

Question

A recent discovery has suggested that a gene mutation results in several amino acid substitutions within an active site.The following substitutions have been identified and are each expected to form the active site:  It was also noticed that a coenzyme molecule containing a hydroxyl (-OH)group binds to the mutated protein in approximately the same location as the original serine but does not alter the structure of the protein in anyway.Based on your knowledge of amino acids, enzymes, and catalysis, which of the following is a REASONABLE conclusion?
A)The mutant protein cleaves on the carboxy side of phenylalanine. 
B)The mutant protein cleaves peptide bonds on the carboxy side of glutamate or aspartate. 
C)The mutant protein cleaves peptide bonds on the carboxy side of lysine or arginine. 
D)The mutant protein functions identical to chymotrypsin. 
E)The mutant protein has no function.

Quizplus · Accepted Answer

The fact that the coenzyme binds in a similar location to the original serine suggests that the mutated protein still has catalytic activity. The identified amino acid substitutions suggest that the active site may now be able to cleave peptide bonds on the carboxy side of glutamate or aspartate. There is no evidence to suggest that the mutant protein functions identical to chymotrypsin or has no function, and there is no information to support the other answer choices.

A Recent Discovery Has Suggested That a Gene Mutation Results