Please answer fast Below picture depicts the enzymatic reaction where carboxylesterase mediatedhydrolysis reaction of à hypothetical carboxyl-ester, water molecule is neededfor this reaction step in order to liberate acid metabolite.a. What is the interaction taking place between Glutamate and Histidine?b. If serine is replaced by alanine how the reaction occursC. If Glutamate is replaced by arginine what happens to the reaction?

enzymes are composed of protein molecules (polypeptides), polymers of amino acids, which have…

Answered: Below picture depicts the enzymatic…

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

See similar textbooks

Similar questions

During the inhibition of glycopeptide transpeptidase, a serine from the enzyme reacts with the amide carbonyl of the lactam ring in penicillin antibiotic to form an enzyme - penicillin complex which inactivates the enzyme. The conversion of an amide to an an ester is not normally observed in reactions of carboxylic acid derivatives. Provide an explanation as to why the amide of a penicillin antibiotic can react with the serine of glyopeptide transpeptidase in this unexpected way.
The diagram below shows an outline of the aminotransferase mechanism that skips the specific steps that show how electrons flow when a Schiff base is formed or is hydrolyzed. Using the mechanistic details given below A. Draw the mechanism for Enzyme- PLP Schiff base formation using pyridoxal and the lysine amine group using arrow to indicate electron flow. B.Draw the mechanism for hydrolysis of the Schiff base to form the a-keto acid, which is the reverse of the first reaction.
The amino acid histidine has been found to participate in both acid and base catalysis in many enzymatic reactions. Which of the following describes histidine? A. Its R group acts as proton donor at pH 7.0 B. Its R group acts as electron pair acceptor at pH 7.0 C. Its R group acts as proton acceptor at pH 7.0 D. Its R group helps in the proteolytic activity by acting as both proton donor and proton acceptor at pH 7.0
1 ).Which of the following accurately describes substrate specificity for serine proteases? A.The binding cleft B.Mg2+ metal activated enzyme C.The catalytic triad D.Facilitates redox chemistry E.Stabilizes the transition state 2). Which of the following amino acid residues would not provide a side chain for acid-base catalysis at physiological pH? select all that apply leucine aspartic acid histidine lysine Please answer both correct i will give u upvote.
Suggest the possible class of enzyme (or name of enzyme) for each of theenzyme-catalyzed reactions below. Briefly explain your answer.
Figure 1 shows the catalytic triad of a-chymotrypsin. Identify A, B and C. Describe the subsequent steps of stage 1 and stage 2 of a- chymotrypsin mechanism. Illustrate with diagrams. A B CH2 H-N N: H-O Figure 1
A tetrapeptide on partial hydrolysis gave the dipeptides ala-met, met-gly, gly-val and the tripeptides ala-met-gly and met-val-gly. Which is False? a.Ala will react with 2,4-dinitrofluorobenzene. b.Val is liberated is liberated from enzymatic analysis c.Val is the N-terminal. d.The tetrapeptide is ala-met-gly-val
Two therapeutics, methotrexate and fluorouracil, inhibit the formation of dTMP, at different points in the synthesis. One is a suicide inhibitor and one is a competitive inhibitor. a. What therapeutic applications are there for inhibiting the synthesis of dTTP? (ie. What are they treating?) b. Identify the which molecule is the competitive inhibitor and which one is the suicide inhibitor and explain how you know.
Considering the general structure of penicillins, how are they rendered ineffective? Select one: a. β-Lactamase performs nucleophilic attack of the amide in the penicillin side chain b. β-Lactamase performs nucleophilic attack of the amide in the β-lactam ring and subsequently hydrolyzes this intermediate c. β-Lactamase performs nucleophilic attack of the thiazolidone ring on the carbon next to the electronegative sulfur leading to a covalently inhibited β-Lactamase d. All of these e. None of these
for the following reactions: arrive at the Michaelis menten enzyme kinetics: E+2A <-----k1,k2----->A.E+A reversible A.E+A<------k3,k4------>A 2E reversible A2.E------k5--------> E+CD non-reverisble show all steps
Please answer this step by step with a diagram showing how it happens.
PLP is a cofactor for a number of enzymes involved in amino acid metabolism. Give an example of reaction in which PLP participates in cleavage of the a, b, and c bonds of an amino acid, as diagrammed in shown Fig.

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781319114671

Author:

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

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781319114671

Author:

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

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Fundamentals of General, Organic, and Biological …

Biochemistry

ISBN:

9780134015187

Author:

John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson

Publisher:

PEARSON

SEE MORE TEXTBOOKS

Below picture depicts the enzymatic reaction where carboxylesterase mediated hydrolysis reaction of à hypothetical carboxyl-ester, water molecule is needed for this reaction step in order to liberate acid metabolite.