An enzyme facilitate catalysis by formation of esterbond with an alcoholic substrate. Which amino acidresidues can facilitate such mechanism of catalysis?Select the correct response:Cys and MetLys and ArgSer and TyrGlu and Asp Among the given statements, which one correctlydescribes the "Induced-Fit Model"?Select the correct response:The active site of the enzyme is exactlycompatible with its substrate. However,the enzyme could undergo conformationalchange to accommodate a variety ofother molecules..The active site of the enzyme is notexactly compatible with its substrate.Upon entry in the active site, the enzymechanges in conformation to make a betterfit with the substrate.The active site of the enzyme is notexactly compatible with its substrate.Upon reaction in the active site, theenzyme induces a conformational changein the substrate to form the transitionstate..The active site of the enzyme is exactlycompatible with its substrate.

Ester bond: The bond that is formed by the condensation of alcohol group with a carboxylic acid…

Answered: An enzyme facilitate catalysis by…

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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Similar questions

The enzyme chymotrypsin, catalyses the hydrolysis of nitrophenyl acetate and other acyl esters. Name the amino acid residue, the side chain of the residuee and the type of bonding/linkage involved in the formation of the acyl-enzyme complex during catalysis.
Which of the following is the most probable catalytic triad of an enzyme that follows general acid base catalysis? -Glu-His-Cys -Leu-His-Ser -Glu-Phe-Ser -Asp-His-Ala -Glu-Phe-Ser -Glu-Phe-Ser -Glu-Phe-Ser -Glu-Phe-Ser -Glu-Phe-Ser -
CH₂OH 애 H2COPO 2- ATP OH 1 애 애 어 애 The class of the enzyme catalyzing the reaction shown in this figure is a(n) Choose the one best answer. ligase 매 +ADP 매
The enzyme chymotrypsin, catalyses the hydrolysis of nitrophenyl acetate and pther acyl esters. Name the amino acid residue, the side chain of the residue, and the type of bond/linkage involved in the formation of the acyl-emzyme complex during catalysis.
Describe the two models that explain the behavior of allosteric enzymes. Include thelimitation or advantage of each. Give also an example of each.
A carboxypeptidase is a metalloenyme (its active site contains one or more metal ions essential for the function) that catalyzes the hydrolysis of the peptide bond of the terminal amino acid of a polypeptide chain (where the free carboxyl group occurs). The binding of an L-alanyl-L-tyrosine peptide substrate in the active site of the enzyme is represented in the scheme below: Glu Zn++ COO™ OH H3C CH₂ HC NH IO C H H Poche apolaire -H H O+N: C N H H H NH₂ Arg 145 Туг 248 NB: This scheme gives a planar representation of the spatial structure of the active site where indicated contacts (hatched lines) are supposed to occur in the 3D structure of the enzyme. 1- Describe the interactions that occur between the ligand and amino acid residues of the active site. 2- What would be the impact on the Km value if we replace L-alanyl-L-tyrosine by the following substrates: L-alanyl-L-phenylalanine; L-alanyl-L-aspartate; L-aspartyl-L- tyrosine.
One way of expressing the rate at which an enzyme can catalyze a reaction is to state its turnover number. The turnover number is the maximum number of substrate molecules that can be acted on by one molecule of enzyme per unit of time. The table gives the turnover number of four representative enzymes. Enzyme Substrate Turnover number (per second) Ribonuclease RNA 100 Fumarase fumarate 800 Lactate dehydrogenase lactate 1000 Urease urea 10,000 How many molecules of urea can one molecule of urease act on in 12.0 min ?
When studying the mechanism of the enzymatic reaction, functional groups were found that ensure the connection of the enzyme molecule with the substrate and take a direct part in the act of catalysis. What are these areas of the enzyme formed by these groups called? What functional structures form them and why?
A generalized enzyme active site is shaped like a hemisphere with a radius of 45Å. The active site holds the following amino acids in a homeostatic solution (pH = 7.38): -HAVARILKHAVARILKHAVARILK- Assuming the charge is distributed uniformly along the hemisphere, determine the force at which this active site acts upon a single ATP molecule at the center of the hemisphere.
Use arrow-pushing to show how the glycerol phosphate reacts with the base :B and NAD* to form DHAP. Show the products of the reaction, including the structure of DHAP. The image can be selected for copying and pasting. :B O-H 2. HO-CH-C-CH-O-Pi H H H NAD*
the following is a coenzyme or cofactor involved in enzymatic reaction. identify the biochemical role that S-adenosylmethionine plays within a biochemical tranformation.
Which of the following is false regarding Serine Proteases? O They employ general acid-base catalysis They contain a catalytic Triad of His, Ser, and Asp residues They employ metal ion catalysis O They cleave simple organic ester bonds near larger residues

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An enzyme facilitate catalysis by formation of ester bond with an alcoholic substrate. Which amino acid residues can facilitate such mechanism of catalysis? Select the correct response: Cys and Met Lys and Arg Ser and Tyr Glu and Asp