Proteolytic enzymes

Question 1

break the peptide bonds that maintain the primary protein structure

Answer 1

proteolytic enzymes

Question 2

is an enzyme that hydrolyzes dietary proteins in the small intestine

Answer 2

Chymotrypsin

Question 3

chymotrypsin acts specifically at peptide bonds on the __________ of the peptide bond

Answer 3

carbonyl side

Question 4

The C-terminal amino acids of the peptides released by bond cleavage are

Answer 4

methionine, tyrosine, tryptophan, and phenylalanine

Question 5

The specificity of chymotrypsin depends upon the presence of a

Answer 5

hydrophobic pocket,

Question 6

a cluster of hydrophobic amino acids brought together by the three-dimensional folding of the protein chain.

Answer 6

hydrophobic pocket,

Question 7

The flat aromatic side chains of certain amino acids (tyrosine, tryptophan, phenylalanine) slide into this pocket, providing the binding specificity required for

Answer 7

catalysis at the catalytic site

Question 8

chymotrypsin cleaves the bond between

Answer 8

phenylalanine and glycine, which is the peptide bond on the carbonyl side of amino acids having an aromatic side chain.

Question 9

trypsin, chymotrypsin, and elastase all hydrolyze peptide bonds

Answer 9

The pancreatic serine proteases

Question 10

As the name suggests, they are produced in the ____and subsequently transported to the _____-

Answer 10

pancreas

small intestine

Question 11

These enzymes are the result of

Answer 11

divergen evolution

Question 12

cleaves peptide bonds on the carbonyl side of aromatic amino acids and large, hydrophobic amino acids such as methionine.

Answer 12

Chymotrypsin

Question 13

cleaves peptide bonds on the carbonyl side of basic amino acids.

Answer 13

Trypsin

Question 14

cleaves peptide bonds on the carbonyl side of glycine and alanine.

Answer 14

Elastase