Which of the following statement is FALSE ?pKa values of active site residues can be shifted from typical pKa valuesEnzymes increase KeqNear attack complexes have reacting molecules close enough to form Va der Waals contactsThe transition state contains at least one partial bond.QUESTION 12The angle o in a peptide best describes:O the angle between the two peptide bondsO the angle between the alpha carbon (Ca) and the amideO the angle between the alpha carbon (Ca) and the carbonylO the angle between the alpha carbon (Ca) and its side chainQUESTION 13Investigating how protein subunits come together studies:super- secondary structureClick Save and Submit to save and submit. Click Save All Ansuers to save all anscers7977 Mostly cloody

Enzymes are the proteins that catalyse the reactions by lowering the activation energy of the…

Answered: Which of the following statement is…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter26: Synthesis And Degradation Of Nucleotides

Section: Chapter Questions

Problem 22P

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complete the following mechanism showing the cleavge of the peptide bond for the following cysteine protease reaction. you only need a catalytic dyad for cystein proteases because the pKa of cysteine is low enough (8) and close enough to the pH of 7.4 that is can easily be deprotonated by histidine.
Which of the following is false regarding Serine Proteases? O They employ general acid-base catalysis They contain a catalytic Triad of His, Ser, and Asp residues They employ metal ion catalysis O They cleave simple organic ester bonds near larger residues
The following is the chemical structure of nicotinamide adenine dinucleotides, a coenzyme commonly used in enzymatic reactions. Но 4 HO 0-P-0 *Na "O. `NH2 N 1 "OH H2N OH Which of the indicate regions is the site of the redox activity of this coenzyme? 2.
Why is the covalent intermediate of elastase stable at low pH? The catalytic histidine cannot act as general acid when protonated. O The catalytic histidine cannot act as a general base when protonated. The catalytic serine cannot form a covalent bond to substrate if the pH is below 7.4. O The catalytic serine cannot preferentially form a hydrogen bond with the catalytic histidine at acidic pH, causing these residues to shift out of their catalytically optimal positions.
Draw me the inhibition reaction mechanism of Cysteine Protease Inhibitor (E64). How the epoxide ring is opening because of the reaction with the thiol group of cysteine and what product are being made. Please draw with arrow pushing and also explain the reason of each attack.
Protease is an enzyme that catalyzes the breaking of amide bonds which is very stable at “mild” conditions, namely body temperature and pH 7 (if done in the lab requires hot conditions, concentrated HCl for hours). Some proteases have two aspartic acid residues at their active sites. Write the reaction mechanism (which follows general acid-base catalysis)
Which of the following statements is right? O For a protein-ligand interaction P +LSP•L, 0 = 0.5 when [L] = Kd. all of the answers are correct Peptide bonds are not weak non-covalent interactions. For an enzymatic reaction that follows Michaelis-Menten kinetics, v/Vmax = 0.5, when [S] = KM. The initial rate of an enzyme catalyzed reaction approaches Vmax, as 1/[S] approaches 0.
2
If the substrate for an enzyme catalyzed reaction contained a negative charge, which of the following amino acids would most likely be present in the active site to provide electrostatic destabilization of the ES complex? Leu Val O Asp O LYS QUESTION 15 What is the function of the histidine in the diagram of the mechanism at right with the substrate, a phenylalanine residue? (n) His Asp Nucleophilic affack by water stabilization of a metal ion covalent catalysis electrostatic attraction of the substrate O acid base catalysis 789 Mustly cloudy Click Save and Submit to save and submit. Click Save All Ansuwers to save all answers. here to search
(i) Describe the mechanism of chymotrypsin in cleaving a peptide bond, highlighting the roles of the catalytice triad for the two phases of the catalytic reactions. Explain the significance of the oxyanion hole for the catalysis. (ii) All serine proteases contain the catalytic triad and these amino acids are positioned in the exact same conformation. Since this is true, why do trypsin and chymotrypsin have such different substrate specificity? What features of the enzyme allow for this situation?
The diagram below shows the substrate binding cleft for a protease, providing the substrate structure, and indicating the residues (using one-letter code) that line the four specificity pockets. 1 M F H₂N K R IZ 2 3 P F S W оо E 4 The protease is known to cleave the amide linkage between W and E residues for substrates containing the WEFD sequence. Using 3-letter code with amino acids linked by a "dash" (ex. GLY-ALA), the N-terminal product is A and the C-terminal product is A
2. To the right is a schematic diagram of His $7 the active site in the Michaelis complex of a-chy- motrypsin and a polypeptide substrate. Describe briefly the catalytic or structural roles of the residues listed below: но — Ser 195 (а) Ser195 AA,-C-ÇH-NH-C-ÇH -NH -AAn R R H H. 193 Gly Ser195 (b) His57 (c) NH groups of Gly193 and Ser195 (d) The most favorable side chain R for binding (e) Identify the scissile bond with an arrow, i.e., the bond in the peptide substrate that is cleaved as a result of the catalytic action of the enzyme. You can point to it on the diagram above.

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