Q1: Enzymes use several types of catalytic mechanisms. Differentiate between acid-base catalysis, covalent catalysis, and metalion catalysis.Acid-base catalysistwo part catalytic process (for example,the chymotrypsin mechanism)a covalent bond formsbetween enzyme and substratelowers the energy or stabilizesthe transition state or intermediateCovalent catalysisAnswer Bankmay use amino acids such asaspartate or lysine forprotonation or proton abstractionmay take part in interactionsinvolving Fe²+catalysts may participate inoxidation-reduction reactionsby changes in the oxidation stateMetal ion catalysiscatalyst retains its originalform after reaction occursa proton is transferredbetween enzyme and substrateuses a nucleophilicfunctional groupAlla Zn²+ cofactor may properlyorient the substrate in the activesite through ionic interactions

Enzymes are biocatalysts which increase the rate of biochemical reactions. Substrate molecules bind…

Answered: Acid-base catalysis two part catalytic…

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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. To catalyze a biochemical reaction, an enzyme typically dissociates into additional reactant molecules, thereby increasing the геaction ratе decomposes and releases energy to increase the number of successful collisions between reactant molecules binds temporarily to reactant molecules to lower the activation energy of the reaction drives the reaction to completion by consuming byproducts of the reaction CLEAR ALL
What are enzymes? What distinguishes enzymes from regular chemical catalysts? On the specificity of enzyme action, please comment. Which factor accounts for their specificity the most? Describe the enzyme catalysis mechanism.
Given the active site diagram below, indicate the mechanism(s) of catalysis. 5 HO OH HN OH ΝΗ *HN ΝΗ Zn²+ Acid-base, Metal ion 3 Metal ion, By Approximation Metal ion Acid-Base, By Approximation Acid-base
During chymotrypsin-mediated catalysis, which of the following statements is true? Select any/all answers that apply. O A. A basic (positively-charged) side chain of the substrate polypeptide sits within the oxyanion hole of the enzyme. O B. A basic (positively-charged) side chain of the substrate polypeptide sits within the specificity pocket of the enzyme. O C. Ser195 hydrogen-bonds with the backbone carbonyl group of the substrate polypeptide within the oxyanion hole of the enzyme. O D. All three residues that comprise the catalytic triad of the enzyme interact directly with the substrate polypeptide chain. O E. Both covalent catalysis and acid-base catalysis occur.
A simple enzymatic reaction proceeds as follows. E+S↔E.S→ E+P Derive the Michaelis–Menten equation for this reaction.
In the Enzyme Commission database system, an enzyme with the designation 4.3.2.1 would catalyze which reaction below? Select one: O a. The conversion of an alcohol to an aldehyde O b. The conversion of an alcohol to a phosphate O c. The conversion of an alcohol to an ether o d. The conversion of an alcohol to an alkene A buffer molecule is protonated at pH 9. Adding this buffer to a reaction greatly increases the rate of reaction at pH 9.0. What is true about the reaction? Select one: O a. The buffer is a specific base Ob. It is catalyzed by acid OC. It is catalyzed by base o d. The buffer is a specific acid
The enzyme which catalyzes the reaction below belongs to which enzyme classification? Н.С— ОН HC=0 C=0 Н-С—ОН H,C-0-P-o- || H,C –0-P-0- O Transfera Hydrolase Isomerase Oxidoreductase
Two experiments were performed with the enzymeribonuclease. In experiment 1 the effect of increasingsubstrate concentration on reaction velocity was measured.In experiment 2 the reaction mixtures were identical tothose in experiment 1 except that 0.1 mg of an unknowncompound was added to each tube. Plot the data accordingto the Lineweaver-Burk method. Determine the effect of theunknown compound on the enzyme’s activity. (Substrateconcentration is measured in millimoles per liter. Velocity ismeasured in the change in optical density per hour.)
How many of the following statements are true? Allosteric enzymes display sigmoidal kinetics for plots of V versus [S] Allosteric enzymes exist in T and R states Allosteric enzymes display kinetics that becomes less sigmoidal in the presence of activators
Define enzyme inhibition. Explain in detail the different types of inhibitions with suitable examples
An uncompetitive inhibitor interacts with the enzyme•substrate complex to form a ternarycomplex (ES•I). This equilibrium reaction can be described as follows:ES + I ⇌ ESIModify the simplified kinetic scheme you drew for E + S ⇌ E + P to include this equilibriumexpression
A competitive inhibitor interacts with the free enzyme to form an enzyme•inhibitor complex(E•I). This equilibrium reaction can be described as follows:E + I ⇌ EIModify the simplified kinetic scheme for the reaction E + S ⇌ E + P to include this equilibriumexpression

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