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Chymotrypsin: Quiz


Question 1: These ________ contain an aromatic ring in their sidechain that fits into a 'hydrophobic pocket' (the P1 position) of the enzyme.
MetabolismAmino acid synthesisAmino acidL-DOPA

Question 2: [1] Chymotrypsin preferentially cleaves peptide amide bonds where the carboxyl side of amide bond (the S1 position) is a tyrosine, ________, or phenylalanine.

Question 3: The main substrates of chymotrypsin include tryptophan, tyrosine, phenylalanine, leucine, and ________, which are cleaved at the carboxyl terminal.
MethionineGlutamic acidCysteineSerine

Question 4: Chymotrypsin is a digestive ________ that can perform proteolysis.
ProteinEnzymeCofactor (biochemistry)Enzyme inhibitor

Question 5: On cleavage by ________ into two parts that are still connected via an S-S bond, cleaved chymotrypsinogen molecules can activate each other by removing two small peptides in a trans-proteolysis.
EnteropeptidaseTrypsinProprotein convertase 1Serine protease

Question 6: Chymotrypsin is synthesized in the ________ by protein biosynthesis as a precursor called chymotrypsinogen that is enzymatically inactive.
DigestionLiverPancreasEndocrine system


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