Podcast Beta
Questions and Answers
Chymotrypsin is an enzyme Has a beta barrel structure Produced by the pancreas secreted into the lumen 3 active site amino acids with the other 242 forming a scaffold protein and regulating and localizing the enzyme Is a protease that cleaves peptide bonds Cleaves in a specific manner targeting the carboxy acid of bulky hydrophobic molecules Active site is large enough to contain bulky proteins and lined with hydrophobic residues to facilitate substrate binding Charge relay system Catalytic triad of ______ is: aspartate, serine, histidine MOA of ______ - Binds of substrate to active site - Serine becomes a nucleophile and attacks the carbonyl of the peptide - Water enters active site, first product leaves - Histidine deprotonates the water attacking the serine substrate complex - Second product leaves - Example of a hydrolase Chymotrysinogen - Inactive form of ______ - Requires proteolytic activation Proteolytic cleavage of ______ogen - Chymotrypsinogen is attacked by tyrsin which cleaves aspargine and isoleucine - Arginine interacts with aspartate to stabilize glycine - Glycine stabilizes oxyanion - Conformational change occurs to activate ______.
chymotrypsin
What is the catalytic triad of chymotrypsin?
What is the inactive form of chymotrypsin?
What type of bonds does chymotrypsin cleave?
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What is the primary structure of chymotrypsin?
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Chymotrypsin is an enzyme that cleaves peptide bonds in a non-specific manner.
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Chymotrypsin contains a catalytic triad composed of aspartate, serine, and histidine.
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Chymotrypsinogen is the active form of chymotrypsin.
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Chymotrypsin cleaves peptide bonds targeting the amino acid of bulky hydrophobic molecules.
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The catalytic triad of chymotrypsin is involved in a charge relay system.
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Chymotrypsin is an enzyme that cleaves peptide bonds in a non-specific manner.
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The catalytic triad of chymotrypsin is involved in a charge relay system.
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Chymotrypsinogen is the active form of chymotrypsin.
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Chymotrypsin cleaves peptide bonds targeting the carboxy acid of bulky hydrophobic molecules.
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Proteolytic cleavage of chymotrypsinogen involves tyrosin cleaving asparagine and isoleucine.
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Chymotrypsin contains a catalytic triad composed of aspartate, serine, and histidine.
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Chymotrypsin is a protease that cleaves peptide bonds in a non-specific manner.
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The catalytic triad of chymotrypsin is not involved in a charge relay system.
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Chymotrypsinogen is the active form of chymotrypsin.
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The catalytic triad of chymotrypsin includes aspartate, serine, and arginine.
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