Coenzyme-dependent enzymes can catalyze the general transformations shown below.What would be the best coenzymes to use for the two steps in the scheme, and why? Then, proposean enzyme-catalyzed method for step A to proceed without a coenzyme. Show this enzymecatalyzed mechanism for step A that does not require the coenzyme. You can abbreviate acidicamino acid residues “Enz–B–H” and basic residues “ B–Enz”. (Part B) Coenzyme-dependent enzymes can catalyze the general transformations shown below.What would be the best coenzymes to use for the two steps in the scheme, and why? Then, proposean enzyme-catalyzed method for step A to proceed without a coenzyme. Show this enzyme-catalyzed mechanism for step A that does not require the coenzyme. You can abbreviate acidicamino acid residues "Enz-B-H" and basic residues "B-Enz".ROHR'AROH'R'H₂OR`'R'BR'R'

Coenzymes are the cofactors or the organic molecule which helps the enzymes in catalyzing various…

(Part B) Coenzyme-dependent enzymes can catalyze the general transformations shown below. What would be the best coenzymes to use for the two steps in the scheme, and why? Then, propose an enzyme-catalyzed method for step A to proceed without a coenzyme. Show this enzyme- catalyzed mechanism for step A that does not require the coenzyme. You can abbreviate acidic amino acid residues "Enz-B-H" and basic residues "B-Enz". R OH 'R' A R OH 'R' H₂O R 'R' B R 'R'

(Part B) Coenzyme-dependent enzymes can catalyze the general transformations shown below. What would be the best coenzymes to use for the two steps in the scheme, and why? Then, propose an enzyme-catalyzed method for step A to proceed without a coenzyme. Show this enzyme- catalyzed mechanism for step A that does not require the coenzyme. You can abbreviate acidic amino acid residues "Enz-B-H" and basic residues "B-Enz". R OH 'R' A R OH 'R' H₂O R 'R' B R 'R'

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter22: Gluconeogenesis, Glycogen Metabolism, And The Pentose Phosphate Pathway

Section: Chapter Questions

Problem 23P: Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the...

See similar textbooks

Similar questions

(Part B) Coenzyme-dependent enzymes can catalyze the general transformations shown below. What would be the best coenzymes to use for the two steps in the scheme, and why? Then, propose an enzyme-catalyzed method for step A to proceed without a coenzyme. Show this enzyme- catalyzed mechanism for step A that does not require the coenzyme. You can abbreviate acidic amino acid residues "Enz-B-H" and basic residues "B-Enz". OH 'R' A R OH 'R' H₂O 'R' B 'R'
An example of an enzyme-catalyzed reaction proceeding via a transition-state stabilization mechanism is the hydrolysis of peptides by chymotrypsin while, Lysozyme is often cited as an example of an enzyme which operates by strain mechanism. Discuss both mechanisms in the context of each enzyme.
Beginning with the 1st tetrahedral intermediate, show the complete steps in chymotrypsin mechanism that occurs to form the 2nd chymotrypsin intermediate in the chymotrypsin active site. The substrate for chymotrypsin to be used is Ala-Tyr-Gly. Further, name the amino acid(s) that would be released as a result of the reactions you'd illustrated above.
(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?
Lysozyme is an antibacterial enzyme found in animals. Residues Asp 101 and Arg 114 are required for efficient catalysis, although they are located at some distance from the active site Glu 35 and Asp 52. Substituting Ala for either Asp 101 or Arg 114 does not significantly alter the enzyme's tertiary structure, but significantly reduces its catalytic activity. Explain.
Using the appropriate graph and table above, explain what the N426S mutation appears to be doing to the enzyme’s function. Discuss the kinetic parameter changes and their meaning in this context, not the structure of the enzyme, which was not given to you.
Glutamine affects the regulatory system for E. coli glutamine synthetase so as to promote the adenylylation of glutamine synthetase and inhibit the deadenylylation. Why do these effects make good metabolic sense?
Lysozyme residues Asp 101 and Arg 114 are required for effi cient catalysis, although they are located at some distance from the active site Glu 35 and Asp 52. Substituting Ala for either Asp 101 or Arg 114 does not signifi cantly alter the enzyme’s tertiary structure, but it signifi cantly reduces its catalytic activity. Explain.
Parts of the mechanism for lysozyme are shown below. The catalytic lysozyme residue side chains can be identified as being above and below the polysaccharide chain shown at point A. Complete the missing structures (points B and E) and curly arrows (points A, B, C, D and E) in the mechanism, as well as from the knowledge you have gained, label the catalytic amino acids at point A in your mechanism with their correct name and residue number. A OH R OH O-R H₂C- HO NHAC NHAC E R D OH B R C H RO H3C- ° H₂C- NHAC Y R OH NHAC R R
During chymotrypsin-mediated catalysis, which of the following statements is true? Select any/all answers that apply. A. A basic (positively-charged) side chain of the substrate polypeptide sits within the oxyanion hole of the enzyme. B. A basic (positively-charged) side chain of the substrate polypeptide sits within the specificity pocket of the enzyme. C. Ser195 hydrogen-bonds with the backbone carbonyl group of the substrate polypeptide within the oxyanion hole of the enzyme. D. All three residues that comprise the catalytic triad of the enzyme interact directly with the substrate polypeptide chain. E. Both covalent catalysis and acid-base catalysis occur.
#1 Specify the role each of the following amino acids play within the crystal structure and/or active site for Be as specific as possible, with pictures (and mechanistic arrows) as necessary. His11 Arg140 Glu89 Trp68 #2 Provide a step-wise mechanism for the reaction Bisphosphoglycerate mutase catalyzes, using the amino acids responsible for aiding in catalysis. You do not need to add surrounding amino acids that aid in substrate specificity. (drawn out)
B-lactamase is an enzyme found in many antibiotic-resistant bacteria that hydrolyzes and inactivates antibiotics like penicillin and cephalosporin. The amount of antibiotic hydrolyzed in 1 minute in a 10-ml solution containing purified ß-lactamase was measured as a function of antibiotic concentration. The kinetics of hydrolysis was performed for two antibiotic substrates (A and B). Assume that the concentration of ß-lactamase was kept constant during the assay. 12 Initial Velocity (nanomole/min) 10 8 2 0 10 20 | 30 [Antibiotic] (µm) 40 50 Antibiotic A Antibiotic B a) Based on the enzyme description, what type of enzyme is ß-lactamase? Lyase Isomerase Ligase Hydrolase Oxidoreductase Transferase b) Based on your answer in (a), what other reactant, in addition to the antibiotic substrate, needs to be in the active site of ß-lactamase for the hydrolysis reaction to proceed? c) From the reaction curves above, what is the approximate value of Vmax for the enzyme reaction? (Do not forget the…