Question 4. Consider the protease chymotrypsin. a. What reaction does it normally catalyze? b. Can it...
Consider the protease chymotrypsin. a. What is its normal catalytic activity? b. Can it catalyze the formation of peptide bonds? Why or why not? c. Does it do so normally in the body? Why or why not?
Consider the serine protease, chymotrypsin. Draw the energy diagram of the reaction catalyzed by chymotrypsin and label all relevant points (intermediates, transition states, reactants, products) a. Draw a dipeptide as a general substrate for chymotrypsin, and draw out the mechanism (use arrows!) describing the proteolytic reaction from the beginning until the covalent intermediate (not the tetrahedral intermediate). b.
Please answer section a thru c:
11. Chymotrypsin is a protease, an enzyme that cleaves peptide bonds. a) At pH 2, the enthalpy and entropy of denaturation for chymotrypsin are +418 kJ/mol and +1.32 kJ/mol respectively. Calculate the melting temperature for chymotrypsin. b) Chymotrypsin inhibitor (CI) is a small protein that binds to chymotrypsin with high affinity and prevents protease activity. The dissociation constant for Chymo-CI is 110 PM in a salt free solution. What is the Gibbs free energy...
1) (10 pts) Serine proteases are enzymes that cleave peptide bonds in proteins. Explain using words (drawings OR both) why serine proteases cleave either before or after different amino acid residues. Talk about at least two of the following proteases: Chymotrypsin, Trypsin, or Elastase. mod 2) (10pts) Below is a hypothetical peptide sequence. Give the peptide fragments that will occur by enzymatic degradation using Trypsin and Chymotrypsin DARSKWKSENLIRTY 3) (10 pts) All superfamilies of serine proteases use the catalytic triad...
1. One enzyme will generally catalyze: a. Does not catalyze any reaction b. Only one unique reaction c. Several different reactions d. many different reactions e. none of the above 2. List three experimental conditions which would affect enzyme activity: (six different conditions were done in lab) 3. enzyme Reaction: ------> Ris called: Q is called: 4. One experimental method that would destroy enzyme activity:
Under typical conditions, many essential biochemical reactions
proceed so slowly that life could not exist without the presence of
enzymes. Enzymes increase reaction rates through a wide variety of
mechanisms. These mechanisms generally utilize the following
strategies: improving the nucleophiles and electrophiles present in
the catalytic R groups or substrates; stabilizing the extra
electron density of the leaving group; and stabilizing transition
states. Proteases are enzymes that break down proteins by
hydrolyzing peptide bonds. Chymotrypsin is a protease found in...
18. In the active site of chymotrypsin, what is the major result of the hydrogen bonding of Histidine-57 to Serine-195? a) The pKa of the side chain of the serine is lowered b) It allows the formation of a tetrahedral intermediate between the histidine and the serine. c) It allows chymotrypsin to recognize the appropriate substrate. d) It prevents chymotrypsin from becoming active inside of the cell and allows it to become activated via proteolytic cleavage. It allows for proteolysis...
(a)Explain what is exergonic reaction and what is endergonic reaction? (b) If a reaction is non-spontaneous (for example, synthesis of a peptide link is endergonic), how can we make that reaction possible? ( c) Explain why human body can be viewed as an intricate designed machine?
(a)Explain what is exergonic reaction and what is endergonic reaction? (b) If a reaction is non-spontaneous (for example, synthesis of a peptide link is endergonic), how can we make that reaction possible? ( c) Explain why human body can be viewed as an intricate designed machine?
the enzyme hexokinase can catalyze the following
reaction:
fructose + ATP -> fructose 6 phosphate + adp
if the deltaG of hydrolysis of fructose 6 phosphate to
fructose + Pi is -13.8 kj/mol and hydrolysis of atp to adp + pi is
-30kj/mol, calculate Keq for the reaction above (R = 8.31 j mol-1
K-1, T = 298 k
3a. The enzyme hexokinase can catalyze the following reaction: Fructose + ATP → Fructose-6-phosphate + ADP If the ΔGo of hydrolysis...