Chymotrypsin, trypsin, and elastase all share the same catalytic mechanism, but have different specificities. (a) These proteases are considered serine proteases because the active sites contain...


Chymotrypsin, trypsin, and elastase all share the same catalytic mechanism, but have different<br>specificities.<br>(a) These proteases are considered serine proteases because the active sites contain serine, histidine<br>and aspartate. Describe the roles that each of these amino acid residues play in hydrolyzing protein<br>substrates.<br>(b) The active site pockets of chymotrypsin, trypsin, and elastase are shown in the image below.<br>Based on the image, which side chain of the amino acids would they prefer to cleave respectively, Ala,<br>Arg, or Trp? Explain your answers.<br>Val 216KVal 190<br>Asp 189<br>Chymotrypsin<br>Trypsin<br>Elastase<br>

Extracted text: Chymotrypsin, trypsin, and elastase all share the same catalytic mechanism, but have different specificities. (a) These proteases are considered serine proteases because the active sites contain serine, histidine and aspartate. Describe the roles that each of these amino acid residues play in hydrolyzing protein substrates. (b) The active site pockets of chymotrypsin, trypsin, and elastase are shown in the image below. Based on the image, which side chain of the amino acids would they prefer to cleave respectively, Ala, Arg, or Trp? Explain your answers. Val 216KVal 190 Asp 189 Chymotrypsin Trypsin Elastase

Jun 11, 2022
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