Answer:
The aromatic amino acids; Phenylalanine, Tryptophan, Tyrosine
Amino acids with bulky side chains; Leucine and Methionine
Explanation:
Chymotrypsin is a member of the serine proteases, which is family of enzymes that hydrolyze peptide bonds through the action of an active site serine.
Chymotrypsin cleaves peptide bonds on the C-terminal of aromatic amino acids or amino acids with bulky hydrophobic sides chains such as phenylalanine, tyrosine and tryptophan, leucine and methionine. This specificity for aromatic amino acids is due to its large hydrophobic pocket and due to the complementary nature of these amino acids when they bind to the pocket.
Answer:
It means that one either exactly resembles a parent or it does not.
Explanation:
Answer:
D) cofactor necessary for enzyme activity.
Explanation:
Carboxypeptidase is an enzyme found in the digestive system whose function is to hydrolyze a peptide bond in the terminal carbon of a protein. Said enzyme contains a zinc atom in its active site and when losing a zinc atom it would lead to loss of the activity of the enzyme, making it of great importance for the activity of the enzyme.
You gotta put the choices how am I going to know what to answer now