Select one or more:O a. forming a covalent bond with the substrate.O b. coordinating a water molecule to make it more acidic.O c. stabilizing an oxyanion.O d. abstracting a proton from the substrate.CheckMatch the following mechanistic roles with the amino acid that can best fulfill thatrole. Each amino acid is used once.Required to form an imine (Schiff base) intermediateLys (neutral)An excellent metal ligand when deprotonatedLys (neutral)Could stabilize the oxyanion intermediate in an acylChoose...exchange mechanismCan act as an acid to protonate a leaving groupChoose...CheckA mutation results in the change of Ser to Asp in the active site of chymotrypsin.Most likely, the mutant enzyme willSelect one:О а.no longer catalyze the hydrolysis of a peptide bond because Asp is notas strong of a nucleophile.O b. preferentially hydrolyze substrates containing phenylalanine.O c. preferentially hydrolyze substrates containing lysine.O d. no longer catalyze the hydrolysis of a peptide bond because Asp isunable to be deprotonated by His57.

>serine protease Catalyzes the hydrolysis of peptide bonds, on the carboxyl side of bulky…

Answered: A mutation results in the change of Ser…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Draw a stepwise mechanism for the following reaction. The fourmemberedring in the starting material and product is called a β-lactam.This functional group confers biological activity on penicillin and many related antibiotics. (Hint: The mechanism begins with β elimination and involves only two steps.)
A1
7. An enzyme-catalyzed reaction proceeds by the mechanism below: E+S1ES --2E+P E+A 3 EA EA+S4→ EAS --5→ EA + P E+I6 → EI EAS +17→ EAIS -8 EIS + P A. B. C. E = enzyme, S = substrate, I = inhibitor, P = product and A = activator Rate constants (k's) for the forward reactions are: K1, K2, k3, K4, k5, k6, k7, and k8 Rate constants (k's) for the reverse reactions are: k-1, k-3, K.4, k.6, and k.7 Write the enzyme balance for this mechanism. How many total equations will result from applying the RAPID EQUILIBRIUM ASSUMPTION? Using any concentrations of species in the mechanism and any of the rate constants (k's), write ONE of the equations that would result from applying the QUASI STEADY STATE ASSUMPTION. (ONLY ONE EQUATION; ANY OF THEM ARE FINE)
The cofactor shown below: is an oxidizing agent is a reducing agent is a carrier of acyl groups is flavin mononucleotide The cofactor shown below: CH2 HC OH HC OH HC OH CH2 H₂C NH H H H OH OH NH₂ 1) is an oxidizing agent 2) is a reducing agent 3) is a carrier of acyl groups 4) is flavin mononucleotide
Which of the following best explains why enzyme catalysis is affected by a change in pH? A. Change in pH alters ionization states of serine in the active site involved in nucleophilic catalysis B. The ionization states of his, asp and glu involved in acid/base catalysis are altered with change in pH C. Change in pH alters ionization states of contact amino acids in the active site D. All enzymes have optimum pH
7
The key regulatory enzyme in pyrimidine synthesis is: a. Aspartate transcarbamoylase. b. Glutamine phosphoribosyl amidotransferase. c. Uridine monophosphate synthetase. d. Orotidylate decarboxylase
Define the following terms:a. proenzymeb. positive cooperativityc. negative cooperativityd. zymogene. free radical
Which of the following mechanisms ensure that the utilization of dietary nucleic acids is effected? A salvage pathway involving the enzymes HGPRT and AGPRT catalyze the transfer of purines to phosphoribosylpyrophosphate Pyrimidines are incorporated directly to phosphoribosyl pyrophosphate. Purines and pyrimidines are synthesized from monomer units which are waste products of metabolism. . Both A and B All of these.
Lysozyme cleaves between NAG and NAM residues in bacterial cell walls and is, therefore, classified as a(an) O A. salt bridge, oxidoreductase O B. peptide bond; hydrolase OC. glycosidic linkage; oxidoreductase O D. glycosidic linkage, hydrolase O E. peptide bond; transferase
Proteases are one of the main drug targets. Choose the False statement regarding proteases. A. Proteases are enzymes that cleave peptide bonds. B. Water is a reactant in the reaction catalyzed by proteases. C. Proteases, like all enzymes show substrate specificity, meaning they cleave only substate that fit the bonding product. D. Proteases rely on the proton transfer from NADH to the substrate. E. Protease mechanism involves only acid-base catalysis.
Small molecules are used as inhibitors of protein action - as drugs. They most often do this by blocking the active site within the protein. Potential drugs can be screened computationally to determine if they are strongly bound to the protein. Figure 1 shows a possible conformation of a candidate drug molecule, 4-bromo-2- carboxymethylamide-pyrrole (abbreviation: BCMAP) at the active site of a protein (abbreviation: PR). Figure 2 shows the full protein structure whilst figure 3 shows a known inhibitor of the protein at the site, overlayed with another calculated conformer of BCMAP. (a) Explain what types of interactions, both intermolecular and intramolecular, that a molecular mechanics forcefield must be able to describe in order to be able to accurately determine the geometry of BCMAP in the protein. Identify which interactions will be the most important to describe accurately. Figure 1.4-bromo-2-carboxymethylamide-pyrrole (BCMAP) (C, N, O, and Br atoms in yellow, blue, red, and…

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