If a serine protease has a moderately deep but very wide hydrophobic pocket within the active site, which substrate amino acid side chains likely are found there during catalysis. List all that apply. Use single letter codes (in capitals) in alphabetical order.
Serine proteases are the enzymes which cleave the peptide bond in proteins by using a serine residue as a nucleophile.
Serine proteases include trypsin, chymotrypsin, and elastase. Chymotrypsin has an active site containing a deep hydrophobic pocket where the substrate amino acids, for example, Phenylalanine, Tyrosine, and Tryptophan binds. Thus the side chain of aromatic amino acids can be found there during catalysis. The single letter codes are F, W, and Y.
If a serine protease has a moderately deep but very wide hydrophobic pocket within the active site, which substrate amino acid side chains likely are found there during catalysis. List all that apply....
If a serine protease has a moderately deep but very wide hydrophobic pocket within the active site, which substrate amino acid side chains likely are found there during catalysis. List all that apply. Use single letter codes (in capitals) in alphabetical order.