Esterase hydrolyzes ester bonds. For simplicity, only the amino acids whose side-chainsinteract with the substrate are shown. Each circled interaction is important for the bindingof the substrate to the enzyme.substratex CHH-OCH3CH ZCH, H,CCH,Esteraseactive site(a) Which of the above amino acids, (X, Y or Z) is closest to the N terminus of the primarysequence of the enzyme?(b) You create two mutants (1 & 2) of the enzyme, each of which has two amino acidsubstitutions at the active (substrate-binding) site. You observe that one mutant can bindto the substrate similarly to the wild-type version of the enzyme, whereas the other cannot.Which of the two mutant versions (1 or 2) will probably not bind to the substrate? Explain,in terms of the characteristics of amino acids, why you selected this version.EnzymeWild-typeAmino acids at the active siteXYMutant 1AspYTyrMutant 2XAlaSer

Esterase- group of enzymes which hydrolyses the ester bond from the substrate like acetylcholine,…

Answered: Esterase hydrolyzes ester bonds. For…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter27: Metabolic Integration And Organ Specialization

Section: Chapter Questions

Problem 20P: Figure 27.3 illustrates the response of R (ATP-regenerating) and U (ATP-utilizing) enzymes to energy...

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Catalytic residues are often found in loops between helices or strands for increased mobility duringcatalysis. Is the catalytic Cys predicted to be located in a loop between helices/strands?Are the other two catalytic residues, His and Asn, also found in loops?
In an enzyme's active site, a catalytic histidine residue abstracts a proton from the hydroxyl group of a catalytic serine residue. The catalytic serine then performs a nucleophilic attack on the carbonyl carbon of a peptide bond (on the substrate). The final products of this reaction are a cleaved substrate at the peptide bond, with a new amino group and carboxyl group, and regenerated catalytic residues. In this reaction, the serine residue is displaying what? A. Proximity and Orientation B. Covalent catalysis C. Metal ion catalysis D .A and B E. B and C F. None stated here
The enzymatic activity of lysozyme is optimal at pH 5.2 and decreases above and below this pH value. Lysozyme contains two amino acid residues in the active site essential for catalysis: Glu35 and Asp52. The pK value for the carboxyl side chains of these two residues are 5.9 and 4.5 respectively. What is the ionization state of each residue at the pH optimum of lysozyme? How can the ionization states of these 2 amino acid residues explain the pH-activity profile of lysozyme?
Using the catalytic mechanism of serine proteases, draw and label a reaction coordinate diagram/graph of the chymotrypsin-catalyzed hydrolysis of a peptide bond.
Legend: Blue – wild-type β-galactosidase Red – mutant β-galactosidase _________ a. What is the optimum pH of wild type β-galactosidase? _________ b. What is the optimum temperature of mutant β-galactosidase? _________ c. Which enzyme has the greater activity at pH 7.2? _________ d. Which enzyme has the greater activity at a temperature of 42.5oC? _________ e. Which enzyme has greater activity if pH decreases from 7.5 to 6.4? _________ f. Which enzyme has greater activity if temperature increases from 40oC to 41 oC?
Why do structural analogs of the transition-state intermediate of an enzyme inhibit the enzyme competitively and with low Ki values (binds tightly)?
Lysozyme is an enzyme that hydrolyzes bacterial cell wall polysaccharides. When this reaction is carried out in the presence of H218O, it is observed that there is retention of configuration at the C1 carbon of the D site sugar as shown below: Would this result suggest that the enzyme mechanism involves the direct nucleophilic attack of water at C1 or that the enzyme mechanism involves attack by a nucleophilic amino acid side chain of the enzyme that generates a transient covalent intermediate?
Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.
Figure 27.3 illustrates the response of R (ATP-regenerating) and U (ATP-utilizing) enzymes to energy charge. a. Would hexokinase be an R enzyme or a U enzyme? Would glutamine: PRPP amidotransferase, the second enzyme in purine biosynthesis, be an R enzyme or a U enzyme? b. If energy charge = 0.5: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low? c. If energy charge = 0.95: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low?
Allosteric Regulation of Ribonucleotide Reductase by ATP and Deoxynucleotides Describe the underlying rationale for the regulatory effects exerted on ribonucleotide reductase by ATP, dATP, dTTP, and dGTP.
Why Do Anabolic and Catabolic Pathways Differ? Why is the pathway for the biosynthesis of a biomolecule at least partially different from the pathway for its catabolism? Why is the pathway for the biosynthesis of a biomolecule inherently more complex than the pathway for its degradation?
Draw the catalytic triad of a serine protease at the first tetrahedryl intermediate stage. Your drawing should include the amino acids that make up the triad, any part of the substrate that should be present, and any other molecules that are present in the active site.

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Esterase hydrolyzes ester bonds. For simplicity, only the amino acids whose side-chains interact with the substrate are shown. Each circled interaction is important for the binding of the substrate to the enzyme.