To answer this question, please reference the Problem Solving Video: pH and pK, of an Amino Acid.Proteases are enzymes that cleave peptide bonds using general acid-base catalysis. General acid-base catalysis relies on a protordonor or acceptor other than water. Proteases rely on proton transfer to create strong nucleophiles from active-site aminoacid residues.In the protease chymotrypsin, an active-site serine is a potent nucleophile. A nearby residue, His 57, interacts with serine toincrease its reactivity. A schematic of chymotrypsin's active site illustrates the active site Ser 195 and His 57 R groups. TheAsp 102 residue helps position the His 57 residue via hydrogen bonding.Asp 102[His][His+]His 576.0-H-NChymotrypsin is a digestive enzyme with a catalytic optimum between pH 7.8 and 8.0. However, due to the presence of gastricjuice, chymotrypsin often functions in an environment of pH 5.5-7.0.IncorrectThe imidazole group of free histidine has a pK₂ of 6.0. Use the Henderson-Hasselbalch equation to determine the ratio ofdeprotonated to protonated His 57 imidazole moieties at pH 6.9.pH = pk₂ + logSer 195OIdentify the ways that His 57 enhances the nucleophilicpower of Ser 195.acid catalystproton acceptorbase catalystproton donor[A][HA]Aside from positioning, what do you think is the role ofthe Asp 102 residue?It allows nucleophilic attack by His 57.It raises the pK, of His 57.It protonates His 57 prior to substrate binding.[His]ratio.[His+]OIt decreases the

Henderson-Hasselbalch equation relates pH, pKa and the ratio of concentrations of protonated to…

Answered: Chymotrypsin is a digestive enzyme with…

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter4: Cells

Section: Chapter Questions

Problem 1ITD

See similar textbooks

Similar questions

The following data describe the catalysis of cleavage of peptide bonds in small peptides by the enzyme UTSAse (the arrow indicates the peptide bond cleaved in each case). Substrate Km(mM) kcat(s-1) PAPA↓G 4.0 26 PAPA↓A 1.5 37 PAPA↓F 0.64 18 what features of amino acid sequence dictate the specificity of the proteolytic cleavage? Large hydrophilic R-groups Large hydrophobic R-groups Neutral R-groups Small hydrophilic R-groups Large hydrophobic R-groups Negatively charged R-groups Positively charged R-groups
Using the catalytic mechanism of serine proteases, draw and label a reaction coordinate diagram/graph of the chymotrypsin-catalyzed hydrolysis of a peptide bond.
Proteases are enzymes that cleave peptide bonds using general acid–base catalysis. General acid–base catalysis relies on a proton donor or acceptor other than water. Proteases rely on proton transfer to create strong nucleophiles from active-site amino acid residues. In the protease chymotrypsin, an active-site serine is a potent nucleophile. A nearby residue, His 57, interacts with serine to increase its reactivity. A schematic of chymotrypsin’s active site illustrates the active site Ser 195 and His 57 R groups. The Asp 102 residue helps position the His 57 residue via hydrogen bonding.
Here is a putative peptide sequence (position number on top of residues): 1 2 3 4 5 6 7 8 9 10 11 12 13 NH2- G C G N V T H N Q C V L S -COOH If expressed in a eukaryotic cell (please mark your answer in the blank space): Position(s) ___ could be N-glycosylated Position(s) ___ could be modified with myristic acid and the bond formed would be a ______________ Position(s) ______and _____ could be modified with palmiti c acid and the bond formed would be a ______________ Positio n(s) ________ could be a segment of a lipid-linked protein with a farnesyl anchor and the bond formed would be a ______________ Position(s) ________ could be a segment of an O-glycosylated protein Position(s) ________ could be modified with a glycosylphosphatidylinositol (GPI) anchor Position(s) ________ could be phosphorylated
Will rate ASAP Which of the following amino acid residues would not provide a side chain for acid-base catalysis at physiological pH? (Assume pK values of each amino acid are equal to the pK value for the free amino acid in solution.) I. leucine II. lysine III. aspartic acid IV. histidine A) I, II, III B) I, II C) I D) II E) I, III
From the oligopeptide below, write completely the amino acids and/or peptide fragments that resulted from the reaction of chymotrypsin. The amino acids and residues should be represented by the three-letter abbreviation.
3CLpro is a cysteine protease, which are among the most common proteases in biochemistry, however they are a structurally diverse family of enzymes especially in the organization of the active site amino acids. A group of scientists have reported a potential drug molecule based on a binding study using circular dichroism. They report that the molecule binds to the active site. Can the experiment support the claims, why or why not? Which techniques might be used to support this claim?
The highest energy point of the serine protease reaction is the formation of the tetrahedral oxyanion intermediate on the original carbonyl carbon of the scissile peptide bond. True or False? DIPF is an irreversible inhibitor of serine proteases. True or False? The acyl-enzyme intermediate is the transition state of the reaction. True or False? Serine proteases are classified as isomerases. True or False?
From the oligopeptide below, write completely the amino acids and/or peptide fragments that resulted from the reaction of trypsin. The amino acids and residues should be represented by the three-letter abbreviation.
a protease that cleave peptide bonds adjacent to aspartate and glutamate would likely have an s1 pocket that contain positively charged amino acids true or false
Only a few amino acid residues are actually involved in catalysis in enzymes, yet enzymes are constructed of at least 100 amino acids, and often many more. Suggest some functions for the noncatalytic amino acids.
An active site of a hypothetical serine protease with a peptide substrate bound is shown below: This serine protease has 3 specificity pockets (S1, S2, S1') as shown in the figure above. S1 pocket has a glutamic acid in the bottom, the S2 pocket is small and hydrophobic, and the S1' pocket is deep and hydrophobic. Based on this information you can conclude that R1 is most likely side chain of a. Asp b. Lys c. Lle d. Gly e. Phe

SEE MORE QUESTIONS

Recommended textbooks for you

Biology: The Dynamic Science (MindTap Course List)

Biology

ISBN:

9781305389892

Author:

Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:

Cengage Learning

Biology: The Dynamic Science (MindTap Course List)

Biology

ISBN:

9781305389892

Author:

Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:

Cengage Learning

SEE MORE TEXTBOOKS